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Volumn 66, Issue , 2014, Pages 173-240

Cellular regulation of glucose uptake by glucose transporter GLUT4

Author keywords

Glucose transport; Glucose transporter; GLUT4; Insulin; Insulin resistance; Intracellular retention; Review; Type 2 diabetes

Indexed keywords

GLUCOSE; GLUCOSE TRANSPORTER 4; PROTEIN KINASE B; SNARE PROTEIN;

EID: 84906075429     PISSN: 00652423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-801401-1.00006-2     Document Type: Chapter
Times cited : (71)

References (381)
  • 1
    • 27844483012 scopus 로고    scopus 로고
    • Childhood obesity and type 2 diabetes mellitus
    • Hannon T.S., Rao G., Arslanian S.A. Childhood obesity and type 2 diabetes mellitus. Pediatrics 2005, 116:473-480.
    • (2005) Pediatrics , vol.116 , pp. 473-480
    • Hannon, T.S.1    Rao, G.2    Arslanian, S.A.3
  • 2
    • 84890745230 scopus 로고    scopus 로고
    • Inadequacies of current approaches to prediabetes and diabetes prevention
    • Bergman M. Inadequacies of current approaches to prediabetes and diabetes prevention. Endocrine 2013, 44(3):623-633.
    • (2013) Endocrine , vol.44 , Issue.3 , pp. 623-633
    • Bergman, M.1
  • 3
    • 84890358162 scopus 로고    scopus 로고
    • Diabetes drugs ride a bumpy road
    • Ledford H. Diabetes drugs ride a bumpy road. Nature 2013, 504(7479):198.
    • (2013) Nature , vol.504 , Issue.7479 , pp. 198
    • Ledford, H.1
  • 4
    • 79961009650 scopus 로고    scopus 로고
    • Assessment and treatment of cardiovascular risk in prediabetes: impaired glucose tolerance and impaired fasting glucose
    • DeFronzo R.A., Abdul-Ghani M. Assessment and treatment of cardiovascular risk in prediabetes: impaired glucose tolerance and impaired fasting glucose. Am. J. Cardiol. 2011, 108(3 Suppl.):3B-24B.
    • (2011) Am. J. Cardiol. , vol.108 , Issue.3 SUPPL
    • DeFronzo, R.A.1    Abdul-Ghani, M.2
  • 5
    • 0030839435 scopus 로고    scopus 로고
    • GLUT4 heterozygous knockout mice develop muscle insulin resistance and diabetes
    • Stenbit A.E., Tsao T.S., Li J., Burcelin R., Geenen D.L., Factor S.M., et al. GLUT4 heterozygous knockout mice develop muscle insulin resistance and diabetes. Nat. Med. 1997, 3:1096-1101.
    • (1997) Nat. Med. , vol.3 , pp. 1096-1101
    • Stenbit, A.E.1    Tsao, T.S.2    Li, J.3    Burcelin, R.4    Geenen, D.L.5    Factor, S.M.6
  • 6
    • 0030967868 scopus 로고    scopus 로고
    • Peripheral but not hepatic insulin resistance in mice with one disrupted allele of the glucose transporter type 4 (GLUT4) gene
    • Rossetti L., Stenbit A.E., Chen W., Hu M., Barzilai N., Katz E.B., et al. Peripheral but not hepatic insulin resistance in mice with one disrupted allele of the glucose transporter type 4 (GLUT4) gene. J. Clin. Invest. 1997, 100(7):1831-1839.
    • (1997) J. Clin. Invest. , vol.100 , Issue.7 , pp. 1831-1839
    • Rossetti, L.1    Stenbit, A.E.2    Chen, W.3    Hu, M.4    Barzilai, N.5    Katz, E.B.6
  • 7
    • 0034078910 scopus 로고    scopus 로고
    • Reduced glucose uptake precedes insulin signaling defects in adipocytes from heterozygous GLUT4 knockout mice
    • Li J., Houseknecht K.L., Stenbit A.E., Katz E.B., Charron M.J. Reduced glucose uptake precedes insulin signaling defects in adipocytes from heterozygous GLUT4 knockout mice. FASEB J. 2000, 14(9):1117-1125.
    • (2000) FASEB J. , vol.14 , Issue.9 , pp. 1117-1125
    • Li, J.1    Houseknecht, K.L.2    Stenbit, A.E.3    Katz, E.B.4    Charron, M.J.5
  • 8
    • 0035825643 scopus 로고    scopus 로고
    • Adipose-selective targeting of the GLUT4 gene impairs insulin action in muscle and liver
    • Abel E.D., Peroni O., Kim J.K., Kim Y.B., Boss O., Hadro E., et al. Adipose-selective targeting of the GLUT4 gene impairs insulin action in muscle and liver. Nature 2001, 409:729-733.
    • (2001) Nature , vol.409 , pp. 729-733
    • Abel, E.D.1    Peroni, O.2    Kim, J.K.3    Kim, Y.B.4    Boss, O.5    Hadro, E.6
  • 9
    • 0033834248 scopus 로고    scopus 로고
    • Targeted disruption of the glucose transporter 4 selectively in muscle causes insulin resistance and glucose intolerance
    • Zisman A., Peroni O.D., Abel E.D., Michael M.D., Mauvais-Jarvis F., Lowell B.B., et al. Targeted disruption of the glucose transporter 4 selectively in muscle causes insulin resistance and glucose intolerance. Nat. Med. 2000, 6:924-928.
    • (2000) Nat. Med. , vol.6 , pp. 924-928
    • Zisman, A.1    Peroni, O.D.2    Abel, E.D.3    Michael, M.D.4    Mauvais-Jarvis, F.5    Lowell, B.B.6
  • 10
    • 0028942658 scopus 로고
    • Glycemic improvement in diabetic db/db mice by overexpression of the human insulin-regulatable glucose transporter (GLUT4)
    • Gibbs E.M., Stock J.L., McCoid S.C., Stukenbrok H.A., Pessin J.E., Stevenson R.W., et al. Glycemic improvement in diabetic db/db mice by overexpression of the human insulin-regulatable glucose transporter (GLUT4). J. Clin. Invest. 1995, 95:1512-1518.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1512-1518
    • Gibbs, E.M.1    Stock, J.L.2    McCoid, S.C.3    Stukenbrok, H.A.4    Pessin, J.E.5    Stevenson, R.W.6
  • 11
    • 0028809116 scopus 로고
    • Expression of an insulin-responsive glucose transporter (GLUT4) minigene in transgenic mice: effect of exercise and role in glucose homeostasis
    • Ikemoto S., Thompson K.S., Itakura H., Lane M.D., Ezaki O. Expression of an insulin-responsive glucose transporter (GLUT4) minigene in transgenic mice: effect of exercise and role in glucose homeostasis. Proc. Natl. Acad. Sci. U.S.A. 1995, 92(3):865-869.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.3 , pp. 865-869
    • Ikemoto, S.1    Thompson, K.S.2    Itakura, H.3    Lane, M.D.4    Ezaki, O.5
  • 12
    • 0030048269 scopus 로고    scopus 로고
    • Improvement of insulin action in diabetic transgenic mice selectively overexpressing GLUT4 in skeletal muscle
    • Leturque A., Loizeau M., Vaulont S., Salminen M., Girard J. Improvement of insulin action in diabetic transgenic mice selectively overexpressing GLUT4 in skeletal muscle. Diabetes 1996, 45:23-27.
    • (1996) Diabetes , vol.45 , pp. 23-27
    • Leturque, A.1    Loizeau, M.2    Vaulont, S.3    Salminen, M.4    Girard, J.5
  • 13
    • 0027363450 scopus 로고
    • Transgenic mice expressing the human GLUT4/muscle-fat facilitative glucose transporter protein exhibit efficient glycemic control
    • Liu M.L., Gibbs E.M., McCoid S.C., Milici A.J., Stukenbrok H.A., McPherson R.K., et al. Transgenic mice expressing the human GLUT4/muscle-fat facilitative glucose transporter protein exhibit efficient glycemic control. Proc. Natl. Acad. Sci. U.S.A. 1993, 90(23):11346-11350.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , Issue.23 , pp. 11346-11350
    • Liu, M.L.1    Gibbs, E.M.2    McCoid, S.C.3    Milici, A.J.4    Stukenbrok, H.A.5    McPherson, R.K.6
  • 14
    • 0035119928 scopus 로고    scopus 로고
    • GLUT4 overexpression in db/db mice dose-dependently ameliorates diabetes but is not a lifelong cure
    • Brozinick J.T., McCoid S.C., Reynolds T.H., Nardone N.A., Hargrove D.M., Stevenson R.W., et al. GLUT4 overexpression in db/db mice dose-dependently ameliorates diabetes but is not a lifelong cure. Diabetes 2001, 50:593-600.
    • (2001) Diabetes , vol.50 , pp. 593-600
    • Brozinick, J.T.1    McCoid, S.C.2    Reynolds, T.H.3    Nardone, N.A.4    Hargrove, D.M.5    Stevenson, R.W.6
  • 15
    • 0030988551 scopus 로고    scopus 로고
    • Amelioration of insulin resistance in streptozotocin diabetic mice by transgenic overexpression of GLUT4 driven by an adipose-specific promoter
    • Tozzo E., Gnudi L., Kahn B.B. Amelioration of insulin resistance in streptozotocin diabetic mice by transgenic overexpression of GLUT4 driven by an adipose-specific promoter. Endocrinology 1997, 138:1604-1611.
    • (1997) Endocrinology , vol.138 , pp. 1604-1611
    • Tozzo, E.1    Gnudi, L.2    Kahn, B.B.3
  • 16
    • 0028961355 scopus 로고
    • High fat diet-induced hyperglycemia: prevention by low level expression of a glucose transporter (GLUT4) minigene in transgenic mice
    • Ikemoto S., Thompson K.S., Takahashi M., Itakura H., Lane M.D., Ezaki O. High fat diet-induced hyperglycemia: prevention by low level expression of a glucose transporter (GLUT4) minigene in transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 1995, 92(8):3096-3099.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.8 , pp. 3096-3099
    • Ikemoto, S.1    Thompson, K.S.2    Takahashi, M.3    Itakura, H.4    Lane, M.D.5    Ezaki, O.6
  • 17
    • 84883705641 scopus 로고    scopus 로고
    • Moderate GLUT4 overexpression improves insulin sensitivity and fasting triglyceridemia in high-fat diet-fed transgenic mice
    • Atkinson B.J., Griesel B.A., King C.D., Josey M.A., Olson A.L. Moderate GLUT4 overexpression improves insulin sensitivity and fasting triglyceridemia in high-fat diet-fed transgenic mice. Diabetes 2013, 62(7):2249-2258.
    • (2013) Diabetes , vol.62 , Issue.7 , pp. 2249-2258
    • Atkinson, B.J.1    Griesel, B.A.2    King, C.D.3    Josey, M.A.4    Olson, A.L.5
  • 18
    • 0029148426 scopus 로고
    • Cardiac and adipose tissue abnormalities but not diabetes in mice deficient in GLUT4
    • Katz E.B., Stenbit A.E., Hatton K., DePinho R., Charron M.J. Cardiac and adipose tissue abnormalities but not diabetes in mice deficient in GLUT4. Nature 1995, 377(6545):151-155.
    • (1995) Nature , vol.377 , Issue.6545 , pp. 151-155
    • Katz, E.B.1    Stenbit, A.E.2    Hatton, K.3    DePinho, R.4    Charron, M.J.5
  • 19
    • 69949101547 scopus 로고    scopus 로고
    • Insulin-stimulated translocation of glucose transporter (GLUT) 12 parallels that of GLUT4 in normal muscle
    • Stuart C.A., Howell M.E., Zhang Y., Yin D. Insulin-stimulated translocation of glucose transporter (GLUT) 12 parallels that of GLUT4 in normal muscle. J. Clin. Endocrinol. Metab. 2009, 94(9):3535-3542.
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , Issue.9 , pp. 3535-3542
    • Stuart, C.A.1    Howell, M.E.2    Zhang, Y.3    Yin, D.4
  • 21
    • 1342327871 scopus 로고    scopus 로고
    • Exercise training reverses insulin resistance in muscle by enhanced recruitment of GLUT-4 to the cell surface
    • 5.1
    • Etgen G.J., Jensen J., Wilson C.M., Hunt D.G., Cushman S.W., Ivy J.L. Exercise training reverses insulin resistance in muscle by enhanced recruitment of GLUT-4 to the cell surface. Am. J. Physiol. 1997, 272(5.1):E864-E869.
    • (1997) Am. J. Physiol. , vol.272
    • Etgen, G.J.1    Jensen, J.2    Wilson, C.M.3    Hunt, D.G.4    Cushman, S.W.5    Ivy, J.L.6
  • 22
    • 0031664854 scopus 로고    scopus 로고
    • Increased GLUT-4 translocation mediates enhanced insulin sensitivity of muscle glucose transport after exercise
    • Hansen P.A., Nolte L.A., Chen M.M., Holloszy J.O. Increased GLUT-4 translocation mediates enhanced insulin sensitivity of muscle glucose transport after exercise. J. Appl. Physiol. 1998, 85(4):1218-1222.
    • (1998) J. Appl. Physiol. , vol.85 , Issue.4 , pp. 1218-1222
    • Hansen, P.A.1    Nolte, L.A.2    Chen, M.M.3    Holloszy, J.O.4
  • 23
    • 0033645010 scopus 로고    scopus 로고
    • Exercise and thiazolidinedione therapy normalize insulin action in the obese Zucker fatty rat
    • Hevener A.L., Reichart D., Olefsky J. Exercise and thiazolidinedione therapy normalize insulin action in the obese Zucker fatty rat. Diabetes 2000, 49(12):2154-2159.
    • (2000) Diabetes , vol.49 , Issue.12 , pp. 2154-2159
    • Hevener, A.L.1    Reichart, D.2    Olefsky, J.3
  • 25
    • 77649189367 scopus 로고    scopus 로고
    • Rosiglitazone increases cell surface GLUT4 levels in 3T3-L1 adipocytes through an enhancement of endosomal recycling
    • Martinez L., Berenguer M., Bruce M.C., Le Marchand-Brustel Y., Govers R. Rosiglitazone increases cell surface GLUT4 levels in 3T3-L1 adipocytes through an enhancement of endosomal recycling. Biochem. Pharmacol. 2010, 79(9):1300-1309.
    • (2010) Biochem. Pharmacol. , vol.79 , Issue.9 , pp. 1300-1309
    • Martinez, L.1    Berenguer, M.2    Bruce, M.C.3    Le Marchand-Brustel, Y.4    Govers, R.5
  • 26
    • 77953598589 scopus 로고    scopus 로고
    • The protein family of glucose transport facilitators: it's not only about glucose after all
    • Augustin R. The protein family of glucose transport facilitators: it's not only about glucose after all. IUBMB Life 2010, 62(5):315-333.
    • (2010) IUBMB Life , vol.62 , Issue.5 , pp. 315-333
    • Augustin, R.1
  • 27
    • 0030046879 scopus 로고    scopus 로고
    • Characterization of a mutant GLUT4 lacking the N-glycosylation site: studies in transfected rat adipose cells
    • Ing B.L., Chen H., Robinson K.A., Buse M.G., Quon M.J. Characterization of a mutant GLUT4 lacking the N-glycosylation site: studies in transfected rat adipose cells. Biochem. Biophys. Res. Commun. 1996, 218:76-82.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 76-82
    • Ing, B.L.1    Chen, H.2    Robinson, K.A.3    Buse, M.G.4    Quon, M.J.5
  • 28
    • 84863207433 scopus 로고    scopus 로고
    • Deciphering the role of GLUT4 N-glycosylation in adipocyte and muscle cell models
    • Zaarour N., Berenguer M., Le Marchand-Brustel Y., Govers R. Deciphering the role of GLUT4 N-glycosylation in adipocyte and muscle cell models. Biochem. J. 2012, 445(2):265-273.
    • (2012) Biochem. J. , vol.445 , Issue.2 , pp. 265-273
    • Zaarour, N.1    Berenguer, M.2    Le Marchand-Brustel, Y.3    Govers, R.4
  • 29
    • 0026316731 scopus 로고
    • The role of N-glycosylation of GLUT1 for glucose transport activity
    • Asano T., Katagiri H., Takata K., Lin J.L., Ishihara H., Inukai K., et al. The role of N-glycosylation of GLUT1 for glucose transport activity. J. Biol. Chem. 1991, 266(36):24632-24636.
    • (1991) J. Biol. Chem. , vol.266 , Issue.36 , pp. 24632-24636
    • Asano, T.1    Katagiri, H.2    Takata, K.3    Lin, J.L.4    Ishihara, H.5    Inukai, K.6
  • 30
    • 0031576545 scopus 로고    scopus 로고
    • Altered N-glycosylation of glucose transporter-1 associated with radiation-induced tumorigenesis of human cell hybrids
    • Noto Y., Iwazaki A., Nagao J., Sumiyama Y., Redpath J.L., Stanbridge E.J., et al. Altered N-glycosylation of glucose transporter-1 associated with radiation-induced tumorigenesis of human cell hybrids. Biochem. Biophys. Res. Commun. 1997, 240(2):395-398.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , Issue.2 , pp. 395-398
    • Noto, Y.1    Iwazaki, A.2    Nagao, J.3    Sumiyama, Y.4    Redpath, J.L.5    Stanbridge, E.J.6
  • 31
    • 80052400203 scopus 로고    scopus 로고
    • N-glycosylation is critical for the stability and intracellular trafficking of GLUT4 glucose transporter
    • Haga Y., Ishii K., Suzuki T. N-glycosylation is critical for the stability and intracellular trafficking of GLUT4 glucose transporter. J. Biol. Chem. 2011, 286(36):31320-31327.
    • (2011) J. Biol. Chem. , vol.286 , Issue.36 , pp. 31320-31327
    • Haga, Y.1    Ishii, K.2    Suzuki, T.3
  • 32
    • 0141446037 scopus 로고    scopus 로고
    • Tissue-specific ablation of the GLUT4 glucose transporter or the insulin receptor challenges assumptions about insulin action and glucose homeostasis
    • Minokoshi Y., Kahn C.R., Kahn B.B. Tissue-specific ablation of the GLUT4 glucose transporter or the insulin receptor challenges assumptions about insulin action and glucose homeostasis. J. Biol. Chem. 2003, 278:33609-33612.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33609-33612
    • Minokoshi, Y.1    Kahn, C.R.2    Kahn, B.B.3
  • 33
    • 0033199378 scopus 로고    scopus 로고
    • Insulin-sensitive GLUT4 glucose transporters are colocalized with GLUT3-expressing cells and demonstrate a chemically distinct neuron-specific localization in rat brain
    • Apelt J., Mehlhorn G., Schliebs R. Insulin-sensitive GLUT4 glucose transporters are colocalized with GLUT3-expressing cells and demonstrate a chemically distinct neuron-specific localization in rat brain. J. Neurosci. Res. 1999, 57(5):693-705.
    • (1999) J. Neurosci. Res. , vol.57 , Issue.5 , pp. 693-705
    • Apelt, J.1    Mehlhorn, G.2    Schliebs, R.3
  • 34
    • 0030565002 scopus 로고    scopus 로고
    • Expression and localization of insulin-regulatable glucose transporter (GLUT4) in rat brain
    • Kobayashi M., Nikami H., Morimatsu M., Saito M. Expression and localization of insulin-regulatable glucose transporter (GLUT4) in rat brain. Neurosci. Lett. 1996, 213(2):103-106.
    • (1996) Neurosci. Lett. , vol.213 , Issue.2 , pp. 103-106
    • Kobayashi, M.1    Nikami, H.2    Morimatsu, M.3    Saito, M.4
  • 35
    • 0026795125 scopus 로고
    • Insulin-responsive glucose transporter expression in renal microvessels and glomeruli
    • Brosius F.C., Briggs J.P., Marcus R.G., Barac-Nieto M., Charron M.J. Insulin-responsive glucose transporter expression in renal microvessels and glomeruli. Kidney Int. 1992, 42(5):1086-1092.
    • (1992) Kidney Int. , vol.42 , Issue.5 , pp. 1086-1092
    • Brosius, F.C.1    Briggs, J.P.2    Marcus, R.G.3    Barac-Nieto, M.4    Charron, M.J.5
  • 36
    • 84893075800 scopus 로고    scopus 로고
    • Podocyte-specific GLUT4-deficient mice have fewer and larger podocytes and are protected from diabetic nephropathy
    • Guzman J., Jauregui A.N., Merscher-Gomez S., Maiguel D., Muresan C., Mitrofanova A., et al. Podocyte-specific GLUT4-deficient mice have fewer and larger podocytes and are protected from diabetic nephropathy. Diabetes 2014, 63(2):701-714.
    • (2014) Diabetes , vol.63 , Issue.2 , pp. 701-714
    • Guzman, J.1    Jauregui, A.N.2    Merscher-Gomez, S.3    Maiguel, D.4    Muresan, C.5    Mitrofanova, A.6
  • 37
    • 84861215287 scopus 로고    scopus 로고
    • Multiple myeloma exhibits novel dependence on GLUT4, GLUT8, and GLUT11: implications for glucose transporter-directed therapy
    • McBrayer S.K., Cheng J.C., Singhal S., Krett N.L., Rosen S.T., Shanmugam M. Multiple myeloma exhibits novel dependence on GLUT4, GLUT8, and GLUT11: implications for glucose transporter-directed therapy. Blood 2012, 119(20):4686-4697.
    • (2012) Blood , vol.119 , Issue.20 , pp. 4686-4697
    • McBrayer, S.K.1    Cheng, J.C.2    Singhal, S.3    Krett, N.L.4    Rosen, S.T.5    Shanmugam, M.6
  • 38
    • 0141450536 scopus 로고    scopus 로고
    • Estrogen and progesterone up-regulate glucose transporter expression in ZR-75-1 human breast cancer cells
    • Medina R.A., Meneses A.M., Vera J.C., Guzman C., Nualart F., Astuya A., et al. Estrogen and progesterone up-regulate glucose transporter expression in ZR-75-1 human breast cancer cells. Endocrinology 2003, 144(10):4527-4535.
    • (2003) Endocrinology , vol.144 , Issue.10 , pp. 4527-4535
    • Medina, R.A.1    Meneses, A.M.2    Vera, J.C.3    Guzman, C.4    Nualart, F.5    Astuya, A.6
  • 39
    • 70349285955 scopus 로고    scopus 로고
    • Insulin-stimulated translocation of GLUT4 to the plasma membrane in rat hippocampus is PI3-kinase dependent
    • Grillo C.A., Piroli G.G., Hendry R.M., Reagan L.P. Insulin-stimulated translocation of GLUT4 to the plasma membrane in rat hippocampus is PI3-kinase dependent. Brain Res. 2009, 1296:35-45.
    • (2009) Brain Res. , vol.1296 , pp. 35-45
    • Grillo, C.A.1    Piroli, G.G.2    Hendry, R.M.3    Reagan, L.P.4
  • 40
    • 33645883249 scopus 로고    scopus 로고
    • Insulin and leptin induce GLUT4 plasma membrane translocation and glucose uptake in a human neuronal cell line by a phosphatidylinositol 3-kinase-dependent mechanism
    • Benomar Y., Naour N., Aubourg A., Bailleux V., Gertler A., Djiane J., et al. Insulin and leptin induce GLUT4 plasma membrane translocation and glucose uptake in a human neuronal cell line by a phosphatidylinositol 3-kinase-dependent mechanism. Endocrinology 2006, 147(5):2550-2556.
    • (2006) Endocrinology , vol.147 , Issue.5 , pp. 2550-2556
    • Benomar, Y.1    Naour, N.2    Aubourg, A.3    Bailleux, V.4    Gertler, A.5    Djiane, J.6
  • 41
    • 0032954067 scopus 로고    scopus 로고
    • Acute exercise induces GLUT4 translocation in skeletal muscle of normal human subjects and subjects with type 2 diabetes
    • Kennedy J.W., Hirshman M.F., Gervino E.V., Ocel J.V., Forse R.A., Hoenig S.J., et al. Acute exercise induces GLUT4 translocation in skeletal muscle of normal human subjects and subjects with type 2 diabetes. Diabetes 1999, 48:1192-1197.
    • (1999) Diabetes , vol.48 , pp. 1192-1197
    • Kennedy, J.W.1    Hirshman, M.F.2    Gervino, E.V.3    Ocel, J.V.4    Forse, R.A.5    Hoenig, S.J.6
  • 42
    • 0025910841 scopus 로고
    • Pretranslational suppression of a glucose transporter protein causes insulin resistance in adipocytes from patients with non-insulin-dependent diabetes mellitus and obesity
    • Garvey W.T., Maianu L., Huecksteadt T.P., Birnbaum M.J., Molina J.M., Ciaraldi T.P. Pretranslational suppression of a glucose transporter protein causes insulin resistance in adipocytes from patients with non-insulin-dependent diabetes mellitus and obesity. J. Clin. Invest. 1991, 87(3):1072-1081.
    • (1991) J. Clin. Invest. , vol.87 , Issue.3 , pp. 1072-1081
    • Garvey, W.T.1    Maianu, L.2    Huecksteadt, T.P.3    Birnbaum, M.J.4    Molina, J.M.5    Ciaraldi, T.P.6
  • 43
  • 44
    • 0025946462 scopus 로고
    • Decreased in vivo glucose uptake but normal expression of GLUT1 and GLUT4 in skeletal muscle of diabetic rats
    • Kahn B.B., Rossetti L., Lodish H.F., Charron M.J. Decreased in vivo glucose uptake but normal expression of GLUT1 and GLUT4 in skeletal muscle of diabetic rats. J. Clin. Invest. 1991, 87(6):2197-2206.
    • (1991) J. Clin. Invest. , vol.87 , Issue.6 , pp. 2197-2206
    • Kahn, B.B.1    Rossetti, L.2    Lodish, H.F.3    Charron, M.J.4
  • 46
    • 22944434929 scopus 로고    scopus 로고
    • Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes
    • Yang Q., Graham T.E., Mody N., Preitner F., Peroni O.D., Zabolotny J.M., et al. Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes. Nature 2005, 436:356-362.
    • (2005) Nature , vol.436 , pp. 356-362
    • Yang, Q.1    Graham, T.E.2    Mody, N.3    Preitner, F.4    Peroni, O.D.5    Zabolotny, J.M.6
  • 47
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil G.S. Inflammation and metabolic disorders. Nature 2006, 444(7121):860-867.
    • (2006) Nature , vol.444 , Issue.7121 , pp. 860-867
    • Hotamisligil, G.S.1
  • 48
    • 0036217052 scopus 로고    scopus 로고
    • Disordered fat storage and mobilization in the pathogenesis of insulin resistance and type 2 diabetes
    • Lewis G.F., Carpentier A., Adeli K., Giacca A. Disordered fat storage and mobilization in the pathogenesis of insulin resistance and type 2 diabetes. Endocr. Rev. 2002, 23:201-229.
    • (2002) Endocr. Rev. , vol.23 , pp. 201-229
    • Lewis, G.F.1    Carpentier, A.2    Adeli, K.3    Giacca, A.4
  • 49
    • 34250303939 scopus 로고    scopus 로고
    • Key role for ceramides in mediating insulin resistance in human muscle cells
    • Pickersgill L., Litherland G.J., Greenberg A.S., Walker M., Yeaman S.J. Key role for ceramides in mediating insulin resistance in human muscle cells. J. Biol. Chem. 2007, 282(17):12583-12589.
    • (2007) J. Biol. Chem. , vol.282 , Issue.17 , pp. 12583-12589
    • Pickersgill, L.1    Litherland, G.J.2    Greenberg, A.S.3    Walker, M.4    Yeaman, S.J.5
  • 50
    • 84860339683 scopus 로고    scopus 로고
    • AMPK enhances insulin-stimulated GLUT4 regulation via lowering membrane cholesterol
    • Habegger K.M., Hoffman N.J., Ridenour C.M., Brozinick J.T., Elmendorf J.S. AMPK enhances insulin-stimulated GLUT4 regulation via lowering membrane cholesterol. Endocrinology 2012, 153(5):2130-2141.
    • (2012) Endocrinology , vol.153 , Issue.5 , pp. 2130-2141
    • Habegger, K.M.1    Hoffman, N.J.2    Ridenour, C.M.3    Brozinick, J.T.4    Elmendorf, J.S.5
  • 51
    • 84881233030 scopus 로고    scopus 로고
    • Molecular effects of advanced glycation end products on cell signalling pathways, ageing and pathophysiology
    • Nedic O., Rattan S.I., Grune T., Trougakos I.P. Molecular effects of advanced glycation end products on cell signalling pathways, ageing and pathophysiology. Free Radic. Res. 2013, 47(S1):28-38.
    • (2013) Free Radic. Res. , vol.47 , Issue.S1 , pp. 28-38
    • Nedic, O.1    Rattan, S.I.2    Grune, T.3    Trougakos, I.P.4
  • 52
    • 33645860825 scopus 로고    scopus 로고
    • Reactive oxygen species have a causal role in multiple forms of insulin resistance
    • Houstis N., Rosen E.D., Lander E.S. Reactive oxygen species have a causal role in multiple forms of insulin resistance. Nature 2006, 440:944-948.
    • (2006) Nature , vol.440 , pp. 944-948
    • Houstis, N.1    Rosen, E.D.2    Lander, E.S.3
  • 53
    • 0027515573 scopus 로고
    • Multiple defects in the adipocyte glucose transport system cause cellular insulin resistance in gestational diabetes. Heterogeneity in the number and a novel abnormality in subcellular localization of GLUT4 glucose transporters
    • Garvey W.T., Maianu L., Zhu J.H., Hancock J.A., Golichowski A.M. Multiple defects in the adipocyte glucose transport system cause cellular insulin resistance in gestational diabetes. Heterogeneity in the number and a novel abnormality in subcellular localization of GLUT4 glucose transporters. Diabetes 1993, 42(12):1773-1785.
    • (1993) Diabetes , vol.42 , Issue.12 , pp. 1773-1785
    • Garvey, W.T.1    Maianu, L.2    Zhu, J.H.3    Hancock, J.A.4    Golichowski, A.M.5
  • 54
    • 0032104120 scopus 로고    scopus 로고
    • Evidence for defects in the trafficking and translocation of GLUT4 glucose transporters in skeletal muscle as a cause of human insulin resistance
    • Garvey W.T., Maianu L., Zhu J.H., Brechtel-Hook G., Wallace P., Baron A.D. Evidence for defects in the trafficking and translocation of GLUT4 glucose transporters in skeletal muscle as a cause of human insulin resistance. J. Clin. Invest. 1998, 101:2377-2386.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2377-2386
    • Garvey, W.T.1    Maianu, L.2    Zhu, J.H.3    Brechtel-Hook, G.4    Wallace, P.5    Baron, A.D.6
  • 55
    • 0035191192 scopus 로고    scopus 로고
    • Adipocytes exhibit abnormal subcellular distribution and translocation of vesicles containing glucose transporter 4 and insulin-regulated aminopeptidase in type 2 diabetes mellitus: implications regarding defects in vesicle trafficking
    • Maianu L., Keller S.R., Garvey W.T. Adipocytes exhibit abnormal subcellular distribution and translocation of vesicles containing glucose transporter 4 and insulin-regulated aminopeptidase in type 2 diabetes mellitus: implications regarding defects in vesicle trafficking. J. Clin. Endocrinol. Metab. 2001, 86:5450-5456.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 5450-5456
    • Maianu, L.1    Keller, S.R.2    Garvey, W.T.3
  • 56
    • 3042841303 scopus 로고    scopus 로고
    • Insulin increases cell surface GLUT4 levels by dose dependently discharging GLUT4 into a cell surface recycling pathway
    • Govers R., Coster A.C., James D.E. Insulin increases cell surface GLUT4 levels by dose dependently discharging GLUT4 into a cell surface recycling pathway. Mol. Cell Biol. 2004, 24:6456-6466.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 6456-6466
    • Govers, R.1    Coster, A.C.2    James, D.E.3
  • 57
    • 84934436733 scopus 로고    scopus 로고
    • High-throughput analysis of the dynamics of recycling cell surface proteins
    • Govers R., James D.E., Coster A.C. High-throughput analysis of the dynamics of recycling cell surface proteins. Methods Mol. Biol. 2008, 440:129-146.
    • (2008) Methods Mol. Biol. , vol.440 , pp. 129-146
    • Govers, R.1    James, D.E.2    Coster, A.C.3
  • 60
    • 61349198937 scopus 로고    scopus 로고
    • Intracellular retention and insulin-stimulated mobilization of GLUT4 glucose transporters
    • Rubin B.R., Bogan J.S. Intracellular retention and insulin-stimulated mobilization of GLUT4 glucose transporters. Vitam. Horm. 2009, 80:155-192.
    • (2009) Vitam. Horm. , vol.80 , pp. 155-192
    • Rubin, B.R.1    Bogan, J.S.2
  • 61
    • 33947596679 scopus 로고    scopus 로고
    • The GLUT4 glucose transporter
    • Huang S., Czech M.P. The GLUT4 glucose transporter. Cell Metab. 2007, 5(4):237-252.
    • (2007) Cell Metab. , vol.5 , Issue.4 , pp. 237-252
    • Huang, S.1    Czech, M.P.2
  • 62
    • 0033609911 scopus 로고    scopus 로고
    • Identification of wortmannin-sensitive targets in 3T3-L1 adipocytes. Dissociation of insulin-stimulated glucose uptake and GLUT4 translocation
    • Hausdorff S.F., Fingar D.C., Morioka K., Garza L.A., Whiteman E.L., Summers S.A., et al. Identification of wortmannin-sensitive targets in 3T3-L1 adipocytes. Dissociation of insulin-stimulated glucose uptake and GLUT4 translocation. J. Biol. Chem. 1999, 274:24677-24684.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24677-24684
    • Hausdorff, S.F.1    Fingar, D.C.2    Morioka, K.3    Garza, L.A.4    Whiteman, E.L.5    Summers, S.A.6
  • 63
    • 0037432053 scopus 로고    scopus 로고
    • A long search for GLUT4 activation
    • Kandror K.V. A long search for GLUT4 activation. Sci. STKE 2003, 2003:E5.
    • (2003) Sci. STKE , vol.2003
    • Kandror, K.V.1
  • 64
    • 0016693548 scopus 로고
    • An established preadipose cell line and its differentiation in culture. II. Factors affecting the adipose conversion
    • Green H., Kehinde O. An established preadipose cell line and its differentiation in culture. II. Factors affecting the adipose conversion. Cell 1975, 5(1):19-27.
    • (1975) Cell , vol.5 , Issue.1 , pp. 19-27
    • Green, H.1    Kehinde, O.2
  • 65
    • 0030669618 scopus 로고    scopus 로고
    • Moving GLUT4: the biogenesis and trafficking of GLUT4 storage vesicles
    • Rea S., James D.E. Moving GLUT4: the biogenesis and trafficking of GLUT4 storage vesicles. Diabetes 1997, 46:1667-1677.
    • (1997) Diabetes , vol.46 , pp. 1667-1677
    • Rea, S.1    James, D.E.2
  • 66
    • 0034532975 scopus 로고    scopus 로고
    • Role for the microtubule cytoskeleton in GLUT4 vesicle trafficking and in the regulation of insulin-stimulated glucose uptake
    • Fletcher L.M., Welsh G.I., Oatey P.B., Tavare J.M. Role for the microtubule cytoskeleton in GLUT4 vesicle trafficking and in the regulation of insulin-stimulated glucose uptake. Biochem. J. 2000, 352(2):267-276.
    • (2000) Biochem. J. , vol.352 , Issue.2 , pp. 267-276
    • Fletcher, L.M.1    Welsh, G.I.2    Oatey, P.B.3    Tavare, J.M.4
  • 67
    • 0742288016 scopus 로고    scopus 로고
    • GLUT4 is retained by an intracellular cycle of vesicle formation and fusion with endosomes
    • Karylowski O., Zeigerer A., Cohen A., McGraw T.E. GLUT4 is retained by an intracellular cycle of vesicle formation and fusion with endosomes. Mol. Biol. Cell 2004, 15:870-882.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 870-882
    • Karylowski, O.1    Zeigerer, A.2    Cohen, A.3    McGraw, T.E.4
  • 68
    • 0029887964 scopus 로고    scopus 로고
    • Compartment ablation analysis of the insulin-responsive glucose transporter (GLUT4) in 3T3-L1 adipocytes
    • Livingstone C., James D.E., Rice J.E., Hanpeter D., Gould G.W. Compartment ablation analysis of the insulin-responsive glucose transporter (GLUT4) in 3T3-L1 adipocytes. Biochem. J. 1996, 315:487-495.
    • (1996) Biochem. J. , vol.315 , pp. 487-495
    • Livingstone, C.1    James, D.E.2    Rice, J.E.3    Hanpeter, D.4    Gould, G.W.5
  • 69
    • 18844405437 scopus 로고    scopus 로고
    • Insulin stimulates the halting, tethering, and fusion of mobile GLUT4 vesicles in rat adipose cells
    • Lizunov V.A., Matsumoto H., Zimmerberg J., Cushman S.W., Frolov V.A. Insulin stimulates the halting, tethering, and fusion of mobile GLUT4 vesicles in rat adipose cells. J. Cell Biol. 2005, 169(3):481-489.
    • (2005) J. Cell Biol. , vol.169 , Issue.3 , pp. 481-489
    • Lizunov, V.A.1    Matsumoto, H.2    Zimmerberg, J.3    Cushman, S.W.4    Frolov, V.A.5
  • 70
    • 84886998869 scopus 로고    scopus 로고
    • Neurotransmitter release: the last millisecond in the life of a synaptic vesicle
    • Sudhof T.C. Neurotransmitter release: the last millisecond in the life of a synaptic vesicle. Neuron 2013, 80(3):675-690.
    • (2013) Neuron , vol.80 , Issue.3 , pp. 675-690
    • Sudhof, T.C.1
  • 71
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg K.J., Rowley N., Kaiser C.A. Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J. Cell Biol. 1997, 137:1469-1482.
    • (1997) J. Cell Biol. , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 72
    • 47649098483 scopus 로고    scopus 로고
    • AQP2 exocytosis in the renal collecting duct-involvement of SNARE isoforms and the regulatory role of Munc18b
    • Procino G., Barbieri C., Tamma G., De Benedictis L., Pessin J.E., Svelto M., et al. AQP2 exocytosis in the renal collecting duct-involvement of SNARE isoforms and the regulatory role of Munc18b. J. Cell Sci. 2008, 121(12):2097-2106.
    • (2008) J. Cell Sci. , vol.121 , Issue.12 , pp. 2097-2106
    • Procino, G.1    Barbieri, C.2    Tamma, G.3    De Benedictis, L.4    Pessin, J.E.5    Svelto, M.6
  • 73
    • 39049171771 scopus 로고    scopus 로고
    • Insulin-induced translocation of CD36 to the plasma membrane is reversible and shows similarity to that of GLUT4
    • van Oort M.M., van Doorn J.M., Bonen A., Glatz J.F., van der Horst D.J., Rodenburg K.W., et al. Insulin-induced translocation of CD36 to the plasma membrane is reversible and shows similarity to that of GLUT4. Biochim. Biophys. Acta 2008, 1781(1-2):61-71.
    • (2008) Biochim. Biophys. Acta , vol.1781 , Issue.1-2 , pp. 61-71
    • van Oort, M.M.1    van Doorn, J.M.2    Bonen, A.3    Glatz, J.F.4    van der Horst, D.J.5    Rodenburg, K.W.6
  • 74
    • 33845973399 scopus 로고    scopus 로고
    • Amino acid transporter ATA2 is stored at the trans-Golgi network and released by insulin stimulus in adipocytes
    • Hatanaka T., Hatanaka Y., Tsuchida J., Ganapathy V., Setou M. Amino acid transporter ATA2 is stored at the trans-Golgi network and released by insulin stimulus in adipocytes. J. Biol. Chem. 2006, 281(51):39273-39284.
    • (2006) J. Biol. Chem. , vol.281 , Issue.51 , pp. 39273-39284
    • Hatanaka, T.1    Hatanaka, Y.2    Tsuchida, J.3    Ganapathy, V.4    Setou, M.5
  • 75
    • 1642463973 scopus 로고    scopus 로고
    • Copper stimulates trafficking of a distinct pool of the Menkes copper ATPase (ATP7A) to the plasma membrane and diverts it into a rapid recycling pool
    • Pase L., Voskoboinik I., Greenough M., Camakaris J. Copper stimulates trafficking of a distinct pool of the Menkes copper ATPase (ATP7A) to the plasma membrane and diverts it into a rapid recycling pool. Biochem. J. 2004, 378(3):1031-1037.
    • (2004) Biochem. J. , vol.378 , Issue.3 , pp. 1031-1037
    • Pase, L.1    Voskoboinik, I.2    Greenough, M.3    Camakaris, J.4
  • 76
    • 33744522161 scopus 로고    scopus 로고
    • Transport of the IgE receptor alpha-chain is controlled by a multicomponent intracellular retention signal
    • Cauvi D.M., Tian X., von Loehneysen K., Robertson M.W. Transport of the IgE receptor alpha-chain is controlled by a multicomponent intracellular retention signal. J. Biol. Chem. 2006, 281(15):10448-10460.
    • (2006) J. Biol. Chem. , vol.281 , Issue.15 , pp. 10448-10460
    • Cauvi, D.M.1    Tian, X.2    von Loehneysen, K.3    Robertson, M.W.4
  • 77
    • 26244449833 scopus 로고    scopus 로고
    • A novel dileucine lysosomal-sorting-signal mediates intracellular EGF-receptor retention independently of protein ubiquitylation
    • Tsacoumangos A., Kil S.J., Ma L., Sonnichsen F.D., Carlin C. A novel dileucine lysosomal-sorting-signal mediates intracellular EGF-receptor retention independently of protein ubiquitylation. J. Cell Sci. 2005, 118(17):3959-3971.
    • (2005) J. Cell Sci. , vol.118 , Issue.17 , pp. 3959-3971
    • Tsacoumangos, A.1    Kil, S.J.2    Ma, L.3    Sonnichsen, F.D.4    Carlin, C.5
  • 78
    • 3142546889 scopus 로고    scopus 로고
    • Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway
    • Belouzard S., Delcroix D., Rouille Y. Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway. J. Biol. Chem. 2004, 279(27):28499-28508.
    • (2004) J. Biol. Chem. , vol.279 , Issue.27 , pp. 28499-28508
    • Belouzard, S.1    Delcroix, D.2    Rouille, Y.3
  • 79
    • 84867051116 scopus 로고    scopus 로고
    • Sorting signals that mediate traffic of chitin synthase III between the TGN/endosomes and to the plasma membrane in yeast
    • Starr T.L., Pagant S., Wang C.W., Schekman R. Sorting signals that mediate traffic of chitin synthase III between the TGN/endosomes and to the plasma membrane in yeast. PLoS One 2012, 7(10):e46386.
    • (2012) PLoS One , vol.7 , Issue.10
    • Starr, T.L.1    Pagant, S.2    Wang, C.W.3    Schekman, R.4
  • 80
    • 0028817838 scopus 로고
    • Cloning and characterization of a novel insulin-regulated membrane aminopeptidase from GLUT4 vesicles
    • Keller S.R., Scott H.M., Mastick C.C., Aebersold R., Lienhard G.E. Cloning and characterization of a novel insulin-regulated membrane aminopeptidase from GLUT4 vesicles. J. Biol. Chem. 1995, 270:23612-23618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23612-23618
    • Keller, S.R.1    Scott, H.M.2    Mastick, C.C.3    Aebersold, R.4    Lienhard, G.E.5
  • 81
    • 0030760971 scopus 로고    scopus 로고
    • The glucose transporter GLUT4 and the aminopeptidase vp165 colocalise in tubulo-vesicular elements in adipocytes and cardiomyocytes
    • Martin S., Rice J.E., Gould G.W., Keller S.R., Slot J.W., James D.E. The glucose transporter GLUT4 and the aminopeptidase vp165 colocalise in tubulo-vesicular elements in adipocytes and cardiomyocytes. J. Cell Sci. 1997, 110:2281-2291.
    • (1997) J. Cell Sci. , vol.110 , pp. 2281-2291
    • Martin, S.1    Rice, J.E.2    Gould, G.W.3    Keller, S.R.4    Slot, J.W.5    James, D.E.6
  • 82
    • 0031561379 scopus 로고    scopus 로고
    • Trafficking kinetics of the insulin-regulated membrane aminopeptidase in 3T3-L1 adipocytes
    • Ross S.A., Herbst J.J., Keller S.R., Lienhard G.E. Trafficking kinetics of the insulin-regulated membrane aminopeptidase in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 1997, 239:247-251.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 247-251
    • Ross, S.A.1    Herbst, J.J.2    Keller, S.R.3    Lienhard, G.E.4
  • 83
    • 79958236857 scopus 로고    scopus 로고
    • Dual-mode of insulin action controls GLUT4 vesicle exocytosis
    • Xu Y., Rubin B.R., Orme C.M., Karpikov A., Yu C., Bogan J.S., et al. Dual-mode of insulin action controls GLUT4 vesicle exocytosis. J. Cell Biol. 2011, 193(4):643-653.
    • (2011) J. Cell Biol. , vol.193 , Issue.4 , pp. 643-653
    • Xu, Y.1    Rubin, B.R.2    Orme, C.M.3    Karpikov, A.4    Yu, C.5    Bogan, J.S.6
  • 84
    • 70350389586 scopus 로고    scopus 로고
    • Variations in the requirement for v-SNAREs in GLUT4 trafficking in adipocytes
    • Zhao P., Yang L., Lopez J.A., Fan J., Burchfield J.G., Bai L., et al. Variations in the requirement for v-SNAREs in GLUT4 trafficking in adipocytes. J. Cell Sci. 2009, 122(19):3472-3480.
    • (2009) J. Cell Sci. , vol.122 , Issue.19 , pp. 3472-3480
    • Zhao, P.1    Yang, L.2    Lopez, J.A.3    Fan, J.4    Burchfield, J.G.5    Bai, L.6
  • 85
    • 73649149038 scopus 로고    scopus 로고
    • Proteomic analysis of GLUT4 storage vesicles reveals LRP1 to be an important vesicle component and target of insulin signaling
    • Jedrychowski M.P., Gartner C.A., Gygi S.P., Zhou L., Herz J., Kandror K.V., et al. Proteomic analysis of GLUT4 storage vesicles reveals LRP1 to be an important vesicle component and target of insulin signaling. J. Biol. Chem. 2010, 285(1):104-114.
    • (2010) J. Biol. Chem. , vol.285 , Issue.1 , pp. 104-114
    • Jedrychowski, M.P.1    Gartner, C.A.2    Gygi, S.P.3    Zhou, L.4    Herz, J.5    Kandror, K.V.6
  • 86
    • 0036325425 scopus 로고    scopus 로고
    • GLUT4 retention in adipocytes requires two intracellular insulin-regulated transport steps
    • Zeigerer A., Lampson M.A., Karylowski O., Sabatini D.D., Adesnik M., Ren M., et al. GLUT4 retention in adipocytes requires two intracellular insulin-regulated transport steps. Mol. Biol. Cell 2002, 13:2421-2435.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2421-2435
    • Zeigerer, A.1    Lampson, M.A.2    Karylowski, O.3    Sabatini, D.D.4    Adesnik, M.5    Ren, M.6
  • 87
    • 0030856712 scopus 로고    scopus 로고
    • Sortilin is a major protein component of GLUT4-containing vesicles
    • Lin B.Z., Pilch P.F., Kandror K.V. Sortilin is a major protein component of GLUT4-containing vesicles. J. Biol. Chem. 1997, 272:24145-24147.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24145-24147
    • Lin, B.Z.1    Pilch, P.F.2    Kandror, K.V.3
  • 89
    • 27844528870 scopus 로고    scopus 로고
    • Characterization of the role of the Rab GTPase-activating protein AS160 in insulin-regulated GLUT4 trafficking
    • Larance M., Ramm G., Stockli J., van Dam E.M., Winata S., Wasinger V., et al. Characterization of the role of the Rab GTPase-activating protein AS160 in insulin-regulated GLUT4 trafficking. J. Biol. Chem. 2005, 280(45):37803-37813.
    • (2005) J. Biol. Chem. , vol.280 , Issue.45 , pp. 37803-37813
    • Larance, M.1    Ramm, G.2    Stockli, J.3    van Dam, E.M.4    Winata, S.5    Wasinger, V.6
  • 90
    • 34247854868 scopus 로고    scopus 로고
    • The luminal Vps10p domain of sortilin plays the predominant role in targeting to insulin-responsive GLUT4-containing vesicles
    • Shi J., Kandror K.V. The luminal Vps10p domain of sortilin plays the predominant role in targeting to insulin-responsive GLUT4-containing vesicles. J. Biol. Chem. 2007, 282(12):9008-9016.
    • (2007) J. Biol. Chem. , vol.282 , Issue.12 , pp. 9008-9016
    • Shi, J.1    Kandror, K.V.2
  • 91
    • 0033988192 scopus 로고    scopus 로고
    • Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes
    • Hashiramoto M., James D.E. Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes. Mol. Cell Biol. 2000, 20:416-427.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 416-427
    • Hashiramoto, M.1    James, D.E.2
  • 92
    • 0035196362 scopus 로고    scopus 로고
    • Insulin-regulated release from the endosomal recycling compartment is regulated by budding of specialized vesicles
    • Lampson M.A., Schmoranzer J., Zeigerer A., Simon S.M., McGraw T.E. Insulin-regulated release from the endosomal recycling compartment is regulated by budding of specialized vesicles. Mol. Biol. Cell 2001, 12:3489-3501.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3489-3501
    • Lampson, M.A.1    Schmoranzer, J.2    Zeigerer, A.3    Simon, S.M.4    McGraw, T.E.5
  • 93
    • 0028584356 scopus 로고
    • A distinct class of intracellular storage vesicles, identified by expression of the glucose transporter GLUT4
    • Herman G.A., Bonzelius F., Cieutat A.M., Kelly R.B. A distinct class of intracellular storage vesicles, identified by expression of the glucose transporter GLUT4. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:12750-12754.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12750-12754
    • Herman, G.A.1    Bonzelius, F.2    Cieutat, A.M.3    Kelly, R.B.4
  • 94
    • 0034909532 scopus 로고    scopus 로고
    • A GLUT4-vesicle marker protein, insulin-responsive aminopeptidase, is localized in a novel vesicular compartment in PC12 cells
    • Thoidis G., Kandror K.V. A GLUT4-vesicle marker protein, insulin-responsive aminopeptidase, is localized in a novel vesicular compartment in PC12 cells. Traffic 2001, 2:577-587.
    • (2001) Traffic , vol.2 , pp. 577-587
    • Thoidis, G.1    Kandror, K.V.2
  • 95
    • 21344439799 scopus 로고    scopus 로고
    • Sortilin is essential and sufficient for the formation of GLUT4 storage vesicles in 3T3-L1 adipocytes
    • Shi J., Kandror K.V. Sortilin is essential and sufficient for the formation of GLUT4 storage vesicles in 3T3-L1 adipocytes. Dev. Cell 2005, 9(1):99-108.
    • (2005) Dev. Cell , vol.9 , Issue.1 , pp. 99-108
    • Shi, J.1    Kandror, K.V.2
  • 96
    • 57649143103 scopus 로고    scopus 로고
    • Self-assembly of GLUT4 storage vesicles during differentiation of 3T3-L1 adipocytes
    • Shi J., Huang G., Kandror K.V. Self-assembly of GLUT4 storage vesicles during differentiation of 3T3-L1 adipocytes. J. Biol. Chem. 2008, 283(44):30311-30321.
    • (2008) J. Biol. Chem. , vol.283 , Issue.44 , pp. 30311-30321
    • Shi, J.1    Huang, G.2    Kandror, K.V.3
  • 97
    • 64149103697 scopus 로고    scopus 로고
    • Involvement of TNF-alpha in abnormal adipocyte and muscle sortilin expression in obese mice and humans
    • Kaddai V., Jager J., Gonzalez T., Najem-Lendom R., Bonnafous S., Tran A., et al. Involvement of TNF-alpha in abnormal adipocyte and muscle sortilin expression in obese mice and humans. Diabetologia 2009, 52(5):932-940.
    • (2009) Diabetologia , vol.52 , Issue.5 , pp. 932-940
    • Kaddai, V.1    Jager, J.2    Gonzalez, T.3    Najem-Lendom, R.4    Bonnafous, S.5    Tran, A.6
  • 98
    • 78049353457 scopus 로고    scopus 로고
    • Palmitate-induced down-regulation of sortilin and impaired GLUT4 trafficking in C2C12 myotubes
    • Tsuchiya Y., Hatakeyama H., Emoto N., Wagatsuma F., Matsushita S., Kanzaki M. Palmitate-induced down-regulation of sortilin and impaired GLUT4 trafficking in C2C12 myotubes. J. Biol. Chem. 2010, 285(45):34371-34381.
    • (2010) J. Biol. Chem. , vol.285 , Issue.45 , pp. 34371-34381
    • Tsuchiya, Y.1    Hatakeyama, H.2    Emoto, N.3    Wagatsuma, F.4    Matsushita, S.5    Kanzaki, M.6
  • 99
    • 77950893000 scopus 로고    scopus 로고
    • GLUT4 is sorted to vesicles whose accumulation beneath and insertion into the plasma membrane are differentially regulated by insulin and selectively affected by insulin resistance
    • Xiong W., Jordens I., Gonzalez E., McGraw T.E. GLUT4 is sorted to vesicles whose accumulation beneath and insertion into the plasma membrane are differentially regulated by insulin and selectively affected by insulin resistance. Mol. Biol. Cell 2010, 21(8):1375-1386.
    • (2010) Mol. Biol. Cell , vol.21 , Issue.8 , pp. 1375-1386
    • Xiong, W.1    Jordens, I.2    Gonzalez, E.3    McGraw, T.E.4
  • 100
    • 77953531316 scopus 로고    scopus 로고
    • Insulin-regulated aminopeptidase is a key regulator of GLUT4 trafficking by controlling the sorting of GLUT4 from endosomes to specialized insulin-regulated vesicles
    • Jordens I., Molle D., Xiong W., Keller S.R., McGraw T.E. Insulin-regulated aminopeptidase is a key regulator of GLUT4 trafficking by controlling the sorting of GLUT4 from endosomes to specialized insulin-regulated vesicles. Mol. Biol. Cell 2010, 21(12):2034-2044.
    • (2010) Mol. Biol. Cell , vol.21 , Issue.12 , pp. 2034-2044
    • Jordens, I.1    Molle, D.2    Xiong, W.3    Keller, S.R.4    McGraw, T.E.5
  • 101
    • 0037124104 scopus 로고    scopus 로고
    • Mice deficient in the insulin-regulated membrane aminopeptidase show substantial decreases in glucose transporter GLUT4 levels but maintain normal glucose homeostasis
    • Keller S.R., Davis A.C., Clairmont K.B. Mice deficient in the insulin-regulated membrane aminopeptidase show substantial decreases in glucose transporter GLUT4 levels but maintain normal glucose homeostasis. J. Biol. Chem. 2002, 277(20):17677-17686.
    • (2002) J. Biol. Chem. , vol.277 , Issue.20 , pp. 17677-17686
    • Keller, S.R.1    Davis, A.C.2    Clairmont, K.B.3
  • 102
    • 34547560123 scopus 로고    scopus 로고
    • The SUMO conjugating enzyme Ubc9 is a regulator of GLUT4 turnover and targeting to the insulin-responsive storage compartment in 3T3-L1 adipocytes
    • Liu L.B., Omata W., Kojima I., Shibata H. The SUMO conjugating enzyme Ubc9 is a regulator of GLUT4 turnover and targeting to the insulin-responsive storage compartment in 3T3-L1 adipocytes. Diabetes 2007, 56(8):1977-1985.
    • (2007) Diabetes , vol.56 , Issue.8 , pp. 1977-1985
    • Liu, L.B.1    Omata, W.2    Kojima, I.3    Shibata, H.4
  • 103
    • 33847701165 scopus 로고    scopus 로고
    • Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase
    • Yeh T.Y., Sbodio J.I., Tsun Z.Y., Luo B., Chi N.W. Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase. Biochem. J. 2007, 402(2):279-290.
    • (2007) Biochem. J. , vol.402 , Issue.2 , pp. 279-290
    • Yeh, T.Y.1    Sbodio, J.I.2    Tsun, Z.Y.3    Luo, B.4    Chi, N.W.5
  • 104
    • 0034806395 scopus 로고    scopus 로고
    • GLUT4 ablation in mice results in redistribution of IRAP to the plasma membrane
    • Jiang H., Li J., Katz E.B., Charron M.J. GLUT4 ablation in mice results in redistribution of IRAP to the plasma membrane. Biochem. Biophys. Res. Commun. 2001, 284:519-525.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 519-525
    • Jiang, H.1    Li, J.2    Katz, E.B.3    Charron, M.J.4
  • 105
    • 0034681365 scopus 로고    scopus 로고
    • Characterization of the insulin-regulated endocytic recycling mechanism in 3T3-L1 adipocytes using a novel reporter molecule
    • Subtil A., Lampson M.A., Keller S.R., McGraw T.E. Characterization of the insulin-regulated endocytic recycling mechanism in 3T3-L1 adipocytes using a novel reporter molecule. J. Biol. Chem. 2000, 275:4787-4795.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4787-4795
    • Subtil, A.1    Lampson, M.A.2    Keller, S.R.3    McGraw, T.E.4
  • 106
    • 2442636649 scopus 로고    scopus 로고
    • GLUT4 overexpression or deficiency in adipocytes of transgenic mice alters the composition of GLUT4 vesicles and the subcellular localization of GLUT4 and insulin-responsive aminopeptidase
    • Carvalho E., Schellhorn S.E., Zabolotny J.M., Martin S., Tozzo E., Peroni O.D., et al. GLUT4 overexpression or deficiency in adipocytes of transgenic mice alters the composition of GLUT4 vesicles and the subcellular localization of GLUT4 and insulin-responsive aminopeptidase. J. Biol. Chem. 2004, 279(20):21598-21605.
    • (2004) J. Biol. Chem. , vol.279 , Issue.20 , pp. 21598-21605
    • Carvalho, E.1    Schellhorn, S.E.2    Zabolotny, J.M.3    Martin, S.4    Tozzo, E.5    Peroni, O.D.6
  • 107
    • 0035341211 scopus 로고    scopus 로고
    • The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein
    • Nielsen M.S., Madsen P., Christensen E.I., Nykjaer A., Gliemann J., Kasper D., et al. The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein. EMBO J. 2001, 20:2180-2190.
    • (2001) EMBO J. , vol.20 , pp. 2180-2190
    • Nielsen, M.S.1    Madsen, P.2    Christensen, E.I.3    Nykjaer, A.4    Gliemann, J.5    Kasper, D.6
  • 108
    • 33845465217 scopus 로고    scopus 로고
    • A specific dileucine motif is required for the GGA-dependent entry of newly synthesized insulin-responsive aminopeptidase into the insulin-responsive compartment
    • Hou J.C., Suzuki N., Pessin J.E., Watson R.T. A specific dileucine motif is required for the GGA-dependent entry of newly synthesized insulin-responsive aminopeptidase into the insulin-responsive compartment. J. Biol. Chem. 2006, 281(44):33457-33466.
    • (2006) J. Biol. Chem. , vol.281 , Issue.44 , pp. 33457-33466
    • Hou, J.C.1    Suzuki, N.2    Pessin, J.E.3    Watson, R.T.4
  • 109
    • 23744486858 scopus 로고    scopus 로고
    • Golgi-localized, gamma-ear-containing, Arf-binding protein adaptors mediate insulin-responsive trafficking of glucose transporter 4 in 3T3-L1 adipocytes
    • Li L.V., Kandror K.V. Golgi-localized, gamma-ear-containing, Arf-binding protein adaptors mediate insulin-responsive trafficking of glucose transporter 4 in 3T3-L1 adipocytes. Mol. Endocrinol. 2005, 19(8):2145-2153.
    • (2005) Mol. Endocrinol. , vol.19 , Issue.8 , pp. 2145-2153
    • Li, L.V.1    Kandror, K.V.2
  • 110
    • 2942616407 scopus 로고    scopus 로고
    • Entry of newly synthesized GLUT4 into the insulin-responsive storage compartment is GGA dependent
    • Watson R.T., Khan A.H., Furukawa M., Hou J.C., Li L., Kanzaki M., et al. Entry of newly synthesized GLUT4 into the insulin-responsive storage compartment is GGA dependent. EMBO J. 2004, 23(10):2059-2070.
    • (2004) EMBO J. , vol.23 , Issue.10 , pp. 2059-2070
    • Watson, R.T.1    Khan, A.H.2    Furukawa, M.3    Hou, J.C.4    Li, L.5    Kanzaki, M.6
  • 111
    • 39849096993 scopus 로고    scopus 로고
    • Discovery and progress in our understanding of the regulated secretory pathway in neuroendocrine cells
    • Morvan J., Tooze S.A. Discovery and progress in our understanding of the regulated secretory pathway in neuroendocrine cells. Histochem. Cell Biol. 2008, 129(3):243-252.
    • (2008) Histochem. Cell Biol. , vol.129 , Issue.3 , pp. 243-252
    • Morvan, J.1    Tooze, S.A.2
  • 112
    • 84890172313 scopus 로고    scopus 로고
    • Lysosomal sorting receptors are essential for secretory granule biogenesis in Tetrahymena
    • Briguglio J.S., Kumar S., Turkewitz A.P. Lysosomal sorting receptors are essential for secretory granule biogenesis in Tetrahymena. J. Cell Biol. 2013, 203(3):537-550.
    • (2013) J. Cell Biol. , vol.203 , Issue.3 , pp. 537-550
    • Briguglio, J.S.1    Kumar, S.2    Turkewitz, A.P.3
  • 113
    • 0032862770 scopus 로고    scopus 로고
    • Signal-mediated sorting to the regulated pathway of protein secretion
    • Gerdes H.H., Glombik M.M. Signal-mediated sorting to the regulated pathway of protein secretion. Ann. Anat. 1999, 181(5):447-453.
    • (1999) Ann. Anat. , vol.181 , Issue.5 , pp. 447-453
    • Gerdes, H.H.1    Glombik, M.M.2
  • 114
    • 0036701575 scopus 로고    scopus 로고
    • Lumenal protein multimerization in the distal secretory pathway/secretory granules
    • Arvan P., Zhang B.Y., Feng L., Liu M., Kuliawat R. Lumenal protein multimerization in the distal secretory pathway/secretory granules. Curr. Opin. Cell Biol. 2002, 14(4):448-453.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , Issue.4 , pp. 448-453
    • Arvan, P.1    Zhang, B.Y.2    Feng, L.3    Liu, M.4    Kuliawat, R.5
  • 115
    • 77953646073 scopus 로고    scopus 로고
    • Secretogranin III: a bridge between core hormone aggregates and the secretory granule membrane
    • Hosaka M., Watanabe T. Secretogranin III: a bridge between core hormone aggregates and the secretory granule membrane. Endocr. J. 2010, 57(4):275-286.
    • (2010) Endocr. J. , vol.57 , Issue.4 , pp. 275-286
    • Hosaka, M.1    Watanabe, T.2
  • 116
    • 21544461501 scopus 로고    scopus 로고
    • Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway
    • Chen Z.Y., Ieraci A., Teng H., Dall H., Meng C.X., Herrera D.G., et al. Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway. J. Neurosci. 2005, 25(26):6156-6166.
    • (2005) J. Neurosci. , vol.25 , Issue.26 , pp. 6156-6166
    • Chen, Z.Y.1    Ieraci, A.2    Teng, H.3    Dall, H.4    Meng, C.X.5    Herrera, D.G.6
  • 117
    • 27744584659 scopus 로고    scopus 로고
    • Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step
    • Koumanov F., Jin B., Yang J., Holman G.D. Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step. Cell Metab. 2005, 2(3):179-189.
    • (2005) Cell Metab. , vol.2 , Issue.3 , pp. 179-189
    • Koumanov, F.1    Jin, B.2    Yang, J.3    Holman, G.D.4
  • 118
    • 84861890085 scopus 로고    scopus 로고
    • Regulation of glucose transporter translocation in health and diabetes
    • Bogan J.S. Regulation of glucose transporter translocation in health and diabetes. Annu. Rev. Biochem. 2012, 81:507-532.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 507-532
    • Bogan, J.S.1
  • 119
    • 0142184334 scopus 로고    scopus 로고
    • Functional cloning of TUG as a regulator of GLUT4 glucose transporter trafficking
    • Bogan J.S., Hendon N., McKee A.E., Tsao T.S., Lodish H.F. Functional cloning of TUG as a regulator of GLUT4 glucose transporter trafficking. Nature 2003, 425:727-733.
    • (2003) Nature , vol.425 , pp. 727-733
    • Bogan, J.S.1    Hendon, N.2    McKee, A.E.3    Tsao, T.S.4    Lodish, H.F.5
  • 120
    • 84863621392 scopus 로고    scopus 로고
    • Endoproteolytic cleavage of TUG protein regulates GLUT4 glucose transporter translocation
    • Bogan J.S., Rubin B.R., Yu C., Loffler M.G., Orme C.M., Belman J.P., et al. Endoproteolytic cleavage of TUG protein regulates GLUT4 glucose transporter translocation. J. Biol. Chem. 2012, 287(28):23932-23947.
    • (2012) J. Biol. Chem. , vol.287 , Issue.28 , pp. 23932-23947
    • Bogan, J.S.1    Rubin, B.R.2    Yu, C.3    Loffler, M.G.4    Orme, C.M.5    Belman, J.P.6
  • 121
    • 33947592425 scopus 로고    scopus 로고
    • The glucose transporter 4-regulating protein TUG is essential for highly insulin-responsive glucose uptake in 3T3-L1 adipocytes
    • Yu C., Cresswell J., Loffler M.G., Bogan J.S. The glucose transporter 4-regulating protein TUG is essential for highly insulin-responsive glucose uptake in 3T3-L1 adipocytes. J. Biol. Chem. 2007, 282(10):7710-7722.
    • (2007) J. Biol. Chem. , vol.282 , Issue.10 , pp. 7710-7722
    • Yu, C.1    Cresswell, J.2    Loffler, M.G.3    Bogan, J.S.4
  • 122
    • 0027480990 scopus 로고
    • Effect of insulin on the rates of synthesis and degradation of GLUT1 and GLUT4 glucose transporters in 3T3-L1 adipocytes
    • Sargeant R.J., Paquet M.R. Effect of insulin on the rates of synthesis and degradation of GLUT1 and GLUT4 glucose transporters in 3T3-L1 adipocytes. Biochem. J. 1993, 290:913-919.
    • (1993) Biochem. J. , vol.290 , pp. 913-919
    • Sargeant, R.J.1    Paquet, M.R.2
  • 123
    • 84880058904 scopus 로고    scopus 로고
    • Enhanced fasting glucose turnover in mice with disrupted action of TUG protein in skeletal muscle
    • Loffler M.G., Birkenfeld A.L., Philbrick K.M., Belman J.P., Habtemichael E.N., Booth C.J., et al. Enhanced fasting glucose turnover in mice with disrupted action of TUG protein in skeletal muscle. J. Biol. Chem. 2013, 288(28):20135-20150.
    • (2013) J. Biol. Chem. , vol.288 , Issue.28 , pp. 20135-20150
    • Loffler, M.G.1    Birkenfeld, A.L.2    Philbrick, K.M.3    Belman, J.P.4    Habtemichael, E.N.5    Booth, C.J.6
  • 124
    • 33750982609 scopus 로고    scopus 로고
    • Golgin-160 is required for the Golgi membrane sorting of the insulin-responsive glucose transporter GLUT4 in adipocytes
    • Williams D., Hicks S.W., Machamer C.E., Pessin J.E. Golgin-160 is required for the Golgi membrane sorting of the insulin-responsive glucose transporter GLUT4 in adipocytes. Mol. Biol. Cell 2006, 17(12):5346-5355.
    • (2006) Mol. Biol. Cell , vol.17 , Issue.12 , pp. 5346-5355
    • Williams, D.1    Hicks, S.W.2    Machamer, C.E.3    Pessin, J.E.4
  • 125
    • 58149089468 scopus 로고    scopus 로고
    • CDK5-dependent phosphorylation of the Rho family GTPase TC10(alpha) regulates insulin-stimulated GLUT4 translocation
    • Okada S., Yamada E., Saito T., Ohshima K., Hashimoto K., Yamada M., et al. CDK5-dependent phosphorylation of the Rho family GTPase TC10(alpha) regulates insulin-stimulated GLUT4 translocation. J. Biol. Chem. 2008, 283(51):35455-35463.
    • (2008) J. Biol. Chem. , vol.283 , Issue.51 , pp. 35455-35463
    • Okada, S.1    Yamada, E.2    Saito, T.3    Ohshima, K.4    Hashimoto, K.5    Yamada, M.6
  • 126
    • 0035195395 scopus 로고    scopus 로고
    • Synapsin dispersion and reclustering during synaptic activity
    • Chi P., Greengard P., Ryan T.A. Synapsin dispersion and reclustering during synaptic activity. Nat. Neurosci. 2001, 4:1187-1193.
    • (2001) Nat. Neurosci. , vol.4 , pp. 1187-1193
    • Chi, P.1    Greengard, P.2    Ryan, T.A.3
  • 127
    • 34248192767 scopus 로고    scopus 로고
    • Expression of a synapsin IIb site 1 phosphorylation mutant in 3T3-L1 adipocytes inhibits basal intracellular retention of GLUT4
    • Muretta J.M., Romenskaia I., Cassiday P.A., Mastick C.C. Expression of a synapsin IIb site 1 phosphorylation mutant in 3T3-L1 adipocytes inhibits basal intracellular retention of GLUT4. J. Cell Sci. 2007, 120(7):1168-1177.
    • (2007) J. Cell Sci. , vol.120 , Issue.7 , pp. 1168-1177
    • Muretta, J.M.1    Romenskaia, I.2    Cassiday, P.A.3    Mastick, C.C.4
  • 128
    • 0033638514 scopus 로고    scopus 로고
    • Insulin recruits GLUT4 from specialized VAMP2-carrying vesicles as well as from the dynamic endosomal/trans-Golgi network in rat adipocytes
    • Ramm G., Slot J.W., James D.E., Stoorvogel W. Insulin recruits GLUT4 from specialized VAMP2-carrying vesicles as well as from the dynamic endosomal/trans-Golgi network in rat adipocytes. Mol. Biol. Cell 2000, 11:4079-4091.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4079-4091
    • Ramm, G.1    Slot, J.W.2    James, D.E.3    Stoorvogel, W.4
  • 129
    • 84866347107 scopus 로고    scopus 로고
    • Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes
    • Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., et al. Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes. J. Cell Biol. 2012, 198(4):545-560.
    • (2012) J. Cell Biol. , vol.198 , Issue.4 , pp. 545-560
    • Chen, Y.1    Wang, Y.2    Zhang, J.3    Deng, Y.4    Jiang, L.5    Song, E.6
  • 130
    • 38049174667 scopus 로고    scopus 로고
    • Insulin releases GLUT4 from static storage compartments into cycling endosomes and increases the rate constant for GLUT4 exocytosis
    • Muretta J.M., Romenskaia I., Mastick C.C. Insulin releases GLUT4 from static storage compartments into cycling endosomes and increases the rate constant for GLUT4 exocytosis. J. Biol. Chem. 2008, 283(1):311-323.
    • (2008) J. Biol. Chem. , vol.283 , Issue.1 , pp. 311-323
    • Muretta, J.M.1    Romenskaia, I.2    Mastick, C.C.3
  • 131
    • 0033789981 scopus 로고    scopus 로고
    • Long-term insulin treatment of 3T3-L1 adipocytes results in mis-targeting of GLUT4: implications for insulin-stimulated glucose transport
    • Maier V.H., Gould G.W. Long-term insulin treatment of 3T3-L1 adipocytes results in mis-targeting of GLUT4: implications for insulin-stimulated glucose transport. Diabetologia 2000, 43:1273-1281.
    • (2000) Diabetologia , vol.43 , pp. 1273-1281
    • Maier, V.H.1    Gould, G.W.2
  • 132
    • 78650908321 scopus 로고    scopus 로고
    • A serum factor induces insulin-independent translocation of GLUT4 to the cell surface which is maintained in insulin resistance
    • Berenguer M., Martinez L., Giorgetti-Peraldi S., Le Marchand-Brustel Y., Govers R. A serum factor induces insulin-independent translocation of GLUT4 to the cell surface which is maintained in insulin resistance. PLoS One 2010, 5(12):e15560.
    • (2010) PLoS One , vol.5 , Issue.12
    • Berenguer, M.1    Martinez, L.2    Giorgetti-Peraldi, S.3    Le Marchand-Brustel, Y.4    Govers, R.5
  • 133
    • 76249115787 scopus 로고    scopus 로고
    • Kinetic evidence for unique regulation of GLUT4 trafficking by insulin and AMP-activated protein kinase activators in L6 myotubes
    • Fazakerley D.J., Holman G.D., Marley A., James D.E., Stockli J., Coster A.C. Kinetic evidence for unique regulation of GLUT4 trafficking by insulin and AMP-activated protein kinase activators in L6 myotubes. J. Biol. Chem. 2010, 285(3):1653-1660.
    • (2010) J. Biol. Chem. , vol.285 , Issue.3 , pp. 1653-1660
    • Fazakerley, D.J.1    Holman, G.D.2    Marley, A.3    James, D.E.4    Stockli, J.5    Coster, A.C.6
  • 134
    • 0023930251 scopus 로고
    • Insulin-induced translocation of glucose transporters from post-Golgi compartments to the plasma membrane of 3T3-L1 adipocytes
    • Blok J., Gibbs E.M., Lienhard G.E., Slot J.W., Geuze H.J. Insulin-induced translocation of glucose transporters from post-Golgi compartments to the plasma membrane of 3T3-L1 adipocytes. J. Cell Biol. 1988, 106:69-76.
    • (1988) J. Cell Biol. , vol.106 , pp. 69-76
    • Blok, J.1    Gibbs, E.M.2    Lienhard, G.E.3    Slot, J.W.4    Geuze, H.J.5
  • 135
    • 0030462980 scopus 로고    scopus 로고
    • GLUT4 in cultured skeletal myotubes is segregated from the transferrin receptor and stored in vesicles associated with TGN
    • Ralston E., Ploug T. GLUT4 in cultured skeletal myotubes is segregated from the transferrin receptor and stored in vesicles associated with TGN. J. Cell Sci. 1996, 109:2967-2978.
    • (1996) J. Cell Sci. , vol.109 , pp. 2967-2978
    • Ralston, E.1    Ploug, T.2
  • 136
    • 0033756692 scopus 로고    scopus 로고
    • Effects of insulin on intracellular GLUT4 vesicles in adipocytes: evidence for a secretory mode of regulation
    • Martin S., Millar C.A., Lyttle C.T., Meerloo T., Marsh B.J., Gould G.W., et al. Effects of insulin on intracellular GLUT4 vesicles in adipocytes: evidence for a secretory mode of regulation. J. Cell Sci. 2000, 113:3427-3438.
    • (2000) J. Cell Sci. , vol.113 , pp. 3427-3438
    • Martin, S.1    Millar, C.A.2    Lyttle, C.T.3    Meerloo, T.4    Marsh, B.J.5    Gould, G.W.6
  • 137
    • 0034252865 scopus 로고    scopus 로고
    • Biogenesis of insulin-responsive GLUT4 vesicles is independent of brefeldin A-sensitive trafficking
    • Martin S., Ramm G., Lyttle C.T., Meerloo T., Stoorvogel W., James D.E. Biogenesis of insulin-responsive GLUT4 vesicles is independent of brefeldin A-sensitive trafficking. Traffic 2000, 1:652-660.
    • (2000) Traffic , vol.1 , pp. 652-660
    • Martin, S.1    Ramm, G.2    Lyttle, C.T.3    Meerloo, T.4    Stoorvogel, W.5    James, D.E.6
  • 139
    • 0028351963 scopus 로고
    • Analysis of the co-localization of the insulin-responsive glucose transporter (GLUT4) and the trans Golgi network marker TGN38 within 3T3-L1 adipocytes
    • Martin S., Reaves B., Banting G., Gould G.W. Analysis of the co-localization of the insulin-responsive glucose transporter (GLUT4) and the trans Golgi network marker TGN38 within 3T3-L1 adipocytes. Biochem. J. 1994, 300:743-749.
    • (1994) Biochem. J. , vol.300 , pp. 743-749
    • Martin, S.1    Reaves, B.2    Banting, G.3    Gould, G.W.4
  • 140
    • 0037423287 scopus 로고    scopus 로고
    • GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network
    • Luke M.R., Kjer-Nielsen L., Brown D.L., Stow J.L., Gleeson P.A. GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. J. Biol. Chem. 2003, 278(6):4216-4226.
    • (2003) J. Biol. Chem. , vol.278 , Issue.6 , pp. 4216-4226
    • Luke, M.R.1    Kjer-Nielsen, L.2    Brown, D.L.3    Stow, J.L.4    Gleeson, P.A.5
  • 141
    • 27744468751 scopus 로고    scopus 로고
    • E-cadherin transport from the trans-Golgi network in tubulovesicular carriers is selectively regulated by Golgin-97
    • Lock J.G., Hammond L.A., Houghton F., Gleeson P.A., Stow J.L. E-cadherin transport from the trans-Golgi network in tubulovesicular carriers is selectively regulated by Golgin-97. Traffic 2005, 6(12):1142-1156.
    • (2005) Traffic , vol.6 , Issue.12 , pp. 1142-1156
    • Lock, J.G.1    Hammond, L.A.2    Houghton, F.3    Gleeson, P.A.4    Stow, J.L.5
  • 142
    • 79952803517 scopus 로고    scopus 로고
    • A distinct trans-Golgi network subcompartment for sorting of synaptic and granule proteins in neurons and neuroendocrine cells
    • Park J.J., Gondre-Lewis M.C., Eiden L.E., Loh Y.P. A distinct trans-Golgi network subcompartment for sorting of synaptic and granule proteins in neurons and neuroendocrine cells. J. Cell Sci. 2011, 124(5):735-744.
    • (2011) J. Cell Sci. , vol.124 , Issue.5 , pp. 735-744
    • Park, J.J.1    Gondre-Lewis, M.C.2    Eiden, L.E.3    Loh, Y.P.4
  • 143
    • 0031007807 scopus 로고    scopus 로고
    • Glucose transporter (GLUT-4) is targeted to secretory granules in rat atrial cardiomyocytes
    • Slot J.W., Garruti G., Martin S., Oorschot V., Posthuma G., Kraegen E.W., et al. Glucose transporter (GLUT-4) is targeted to secretory granules in rat atrial cardiomyocytes. J. Cell Biol. 1997, 137:1243-1254.
    • (1997) J. Cell Biol. , vol.137 , pp. 1243-1254
    • Slot, J.W.1    Garruti, G.2    Martin, S.3    Oorschot, V.4    Posthuma, G.5    Kraegen, E.W.6
  • 144
    • 0037341432 scopus 로고    scopus 로고
    • GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in syntaxins 6 and 16 but not TGN38: involvement of an acidic targeting motif
    • Shewan A.M., Van Dam E.M., Martin S., Luen T.B., Hong W., Bryant N.J., et al. GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in syntaxins 6 and 16 but not TGN38: involvement of an acidic targeting motif. Mol. Biol. Cell 2003, 14:973-986.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 973-986
    • Shewan, A.M.1    Van Dam, E.M.2    Martin, S.3    Luen, T.B.4    Hong, W.5    Bryant, N.J.6
  • 146
    • 0037128205 scopus 로고    scopus 로고
    • Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform
    • Mallard F., Tang B.L., Galli T., Tenza D., Saint-Pol A., Yue X., et al. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 2002, 156:653-664.
    • (2002) J. Cell Biol. , vol.156 , pp. 653-664
    • Mallard, F.1    Tang, B.L.2    Galli, T.3    Tenza, D.4    Saint-Pol, A.5    Yue, X.6
  • 148
    • 33745886256 scopus 로고    scopus 로고
    • Syntaxin 16 controls the intracellular sequestration of GLUT4 in 3T3-L1 adipocytes
    • Proctor K.M., Miller S.C., Bryant N.J., Gould G.W. Syntaxin 16 controls the intracellular sequestration of GLUT4 in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 2006, 347(2):433-438.
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , Issue.2 , pp. 433-438
    • Proctor, K.M.1    Miller, S.C.2    Bryant, N.J.3    Gould, G.W.4
  • 149
    • 66349085035 scopus 로고    scopus 로고
    • A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism
    • Vassilopoulos S., Esk C., Hoshino S., Funke B.H., Chen C.Y., Plocik A.M., et al. A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism. Science 2009, 324(5931):1192-1196.
    • (2009) Science , vol.324 , Issue.5931 , pp. 1192-1196
    • Vassilopoulos, S.1    Esk, C.2    Hoshino, S.3    Funke, B.H.4    Chen, C.Y.5    Plocik, A.M.6
  • 150
    • 75749142337 scopus 로고    scopus 로고
    • The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step
    • Esk C., Chen C.Y., Johannes L., Brodsky F.M. The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step. J. Cell Biol. 2010, 188(1):131-144.
    • (2010) J. Cell Biol. , vol.188 , Issue.1 , pp. 131-144
    • Esk, C.1    Chen, C.Y.2    Johannes, L.3    Brodsky, F.M.4
  • 151
    • 81055155979 scopus 로고    scopus 로고
    • Molecular basis of insulin-responsive GLUT4 trafficking systems revealed by single molecule imaging
    • Hatakeyama H., Kanzaki M. Molecular basis of insulin-responsive GLUT4 trafficking systems revealed by single molecule imaging. Traffic 2011, 12(12):1805-1820.
    • (2011) Traffic , vol.12 , Issue.12 , pp. 1805-1820
    • Hatakeyama, H.1    Kanzaki, M.2
  • 152
    • 0034623934 scopus 로고    scopus 로고
    • Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles
    • Chi N.W., Lodish H.F. Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. J. Biol. Chem. 2000, 275:38437-38444.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38437-38444
    • Chi, N.W.1    Lodish, H.F.2
  • 153
    • 19644372736 scopus 로고    scopus 로고
    • P115 Interacts with the GLUT4 vesicle protein, IRAP, and plays a critical role in insulin-stimulated GLUT4 translocation
    • Hosaka T., Brooks C.C., Presman E., Kim S.K., Zhang Z., Breen M., et al. p115 Interacts with the GLUT4 vesicle protein, IRAP, and plays a critical role in insulin-stimulated GLUT4 translocation. Mol. Biol. Cell 2005, 16(6):2882-2890.
    • (2005) Mol. Biol. Cell , vol.16 , Issue.6 , pp. 2882-2890
    • Hosaka, T.1    Brooks, C.C.2    Presman, E.3    Kim, S.K.4    Zhang, Z.5    Breen, M.6
  • 154
    • 84857464993 scopus 로고    scopus 로고
    • The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-Golgi intermediate compartment
    • Orme C.M., Bogan J.S. The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-Golgi intermediate compartment. J. Biol. Chem. 2012, 287(9):6679-6692.
    • (2012) J. Biol. Chem. , vol.287 , Issue.9 , pp. 6679-6692
    • Orme, C.M.1    Bogan, J.S.2
  • 155
    • 84860311872 scopus 로고    scopus 로고
    • The Golgin coiled-coil proteins of the Golgi apparatus
    • Munro S. The Golgin coiled-coil proteins of the Golgi apparatus. Cold Spring Harb. Perspect. Biol. 2011, 3(6):a005256.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , Issue.6
    • Munro, S.1
  • 156
    • 79958257226 scopus 로고    scopus 로고
    • New components of the Golgi matrix
    • Xiang Y., Wang Y. New components of the Golgi matrix. Cell Tissue Res. 2011, 344(3):365-379.
    • (2011) Cell Tissue Res. , vol.344 , Issue.3 , pp. 365-379
    • Xiang, Y.1    Wang, Y.2
  • 157
    • 0029741442 scopus 로고    scopus 로고
    • The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells
    • Martin S., Tellam J., Livingstone C., Slot J.W., Gould G.W., James D.E. The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells. J. Cell Biol. 1996, 134:625-635.
    • (1996) J. Cell Biol. , vol.134 , pp. 625-635
    • Martin, S.1    Tellam, J.2    Livingstone, C.3    Slot, J.W.4    Gould, G.W.5    James, D.E.6
  • 158
    • 0032555928 scopus 로고    scopus 로고
    • Analysis of GLUT4 distribution in whole skeletal muscle fibers: identification of distinct storage compartments that are recruited by insulin and muscle contractions
    • Ploug T., van Deurs B., Ai H., Cushman S.W., Ralston E. Analysis of GLUT4 distribution in whole skeletal muscle fibers: identification of distinct storage compartments that are recruited by insulin and muscle contractions. J. Cell Biol. 1998, 142:1429-1446.
    • (1998) J. Cell Biol. , vol.142 , pp. 1429-1446
    • Ploug, T.1    van Deurs, B.2    Ai, H.3    Cushman, S.W.4    Ralston, E.5
  • 159
    • 0032584674 scopus 로고    scopus 로고
    • Cellubrevin-targeted fluorescence uncovers heterogeneity in the recycling endosomes
    • Teter K., Chandy G., Quinones B., Pereyra K., Machen T., Moore H.P. Cellubrevin-targeted fluorescence uncovers heterogeneity in the recycling endosomes. J. Biol. Chem. 1998, 273:19625-19633.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19625-19633
    • Teter, K.1    Chandy, G.2    Quinones, B.3    Pereyra, K.4    Machen, T.5    Moore, H.P.6
  • 160
    • 0032504203 scopus 로고    scopus 로고
    • Identification of an insulin-responsive, slow endocytic recycling mechanism in Chinese hamster ovary cells
    • Johnson A.O., Subtil A., Petrush R., Kobylarz K., Keller S.R., McGraw T.E. Identification of an insulin-responsive, slow endocytic recycling mechanism in Chinese hamster ovary cells. J. Biol. Chem. 1998, 273:17968-17977.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17968-17977
    • Johnson, A.O.1    Subtil, A.2    Petrush, R.3    Kobylarz, K.4    Keller, S.R.5    McGraw, T.E.6
  • 161
    • 0034472887 scopus 로고    scopus 로고
    • Demonstration of insulin-responsive trafficking of GLUT4 and vpTR in fibroblasts
    • Lampson M.A., Racz A., Cushman S.W., McGraw T.E. Demonstration of insulin-responsive trafficking of GLUT4 and vpTR in fibroblasts. J. Cell Sci. 2000, 113:4065-4076.
    • (2000) J. Cell Sci. , vol.113 , pp. 4065-4076
    • Lampson, M.A.1    Racz, A.2    Cushman, S.W.3    McGraw, T.E.4
  • 162
    • 37849189529 scopus 로고    scopus 로고
    • The luminal domain participates in the endosomal trafficking of the cation-independent mannose 6-phosphate receptor
    • Waguri S., Tomiyama Y., Ikeda H., Hida T., Sakai N., Taniike M., et al. The luminal domain participates in the endosomal trafficking of the cation-independent mannose 6-phosphate receptor. Exp. Cell Res. 2006, 312(20):4090-4107.
    • (2006) Exp. Cell Res. , vol.312 , Issue.20 , pp. 4090-4107
    • Waguri, S.1    Tomiyama, Y.2    Ikeda, H.3    Hida, T.4    Sakai, N.5    Taniike, M.6
  • 163
    • 0035794533 scopus 로고    scopus 로고
    • GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment
    • Chatterjee S., Smith E.R., Hanada K., Stevens V.L., Mayor S. GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment. EMBO J. 2001, 20:1583-1592.
    • (2001) EMBO J. , vol.20 , pp. 1583-1592
    • Chatterjee, S.1    Smith, E.R.2    Hanada, K.3    Stevens, V.L.4    Mayor, S.5
  • 164
    • 0032541423 scopus 로고    scopus 로고
    • Cholesterol-dependent retention of GPI-anchored proteins in endosomes
    • Mayor S., Sabharanjak S., Maxfield F.R. Cholesterol-dependent retention of GPI-anchored proteins in endosomes. EMBO J. 1998, 17:4626-4638.
    • (1998) EMBO J. , vol.17 , pp. 4626-4638
    • Mayor, S.1    Sabharanjak, S.2    Maxfield, F.R.3
  • 165
    • 0029050487 scopus 로고
    • Oligomerized transferrin receptors are selectively retained by a lumenal sorting signal in a long-lived endocytic recycling compartment
    • Marsh E.W., Leopold P.L., Jones N.L., Maxfield F.R. Oligomerized transferrin receptors are selectively retained by a lumenal sorting signal in a long-lived endocytic recycling compartment. J. Cell Biol. 1995, 129(6):1509-1522.
    • (1995) J. Cell Biol. , vol.129 , Issue.6 , pp. 1509-1522
    • Marsh, E.W.1    Leopold, P.L.2    Jones, N.L.3    Maxfield, F.R.4
  • 166
    • 0034677953 scopus 로고    scopus 로고
    • Basic fibroblast growth factor stimulates surface expression and activity of Na(+)/H(+) exchanger NHE3 via mechanism involving phosphatidylinositol 3-kinase
    • Janecki A.J., Janecki M., Akhter S., Donowitz M. Basic fibroblast growth factor stimulates surface expression and activity of Na(+)/H(+) exchanger NHE3 via mechanism involving phosphatidylinositol 3-kinase. J. Biol. Chem. 2000, 275:8133-8142.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8133-8142
    • Janecki, A.J.1    Janecki, M.2    Akhter, S.3    Donowitz, M.4
  • 167
    • 0031890211 scopus 로고    scopus 로고
    • The epithelial sodium-hydrogen antiporter Na+/H+ exchanger 3 accumulates and is functional in recycling endosomes
    • D'Souza S., Garcia-Cabado A., Yu F., Teter K., Lukacs G., Skorecki K., et al. The epithelial sodium-hydrogen antiporter Na+/H+ exchanger 3 accumulates and is functional in recycling endosomes. J. Biol. Chem. 1998, 273:2035-2043.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2035-2043
    • D'Souza, S.1    Garcia-Cabado, A.2    Yu, F.3    Teter, K.4    Lukacs, G.5    Skorecki, K.6
  • 168
    • 33644857424 scopus 로고    scopus 로고
    • GLUT4 distribution between the plasma membrane and the intracellular compartments is maintained by an insulin-modulated bipartite dynamic mechanism
    • Martin O.J., Lee A., McGraw T.E. GLUT4 distribution between the plasma membrane and the intracellular compartments is maintained by an insulin-modulated bipartite dynamic mechanism. J. Biol. Chem. 2006, 281(1):484-490.
    • (2006) J. Biol. Chem. , vol.281 , Issue.1 , pp. 484-490
    • Martin, O.J.1    Lee, A.2    McGraw, T.E.3
  • 169
    • 54249154367 scopus 로고    scopus 로고
    • Molecular mechanisms controlling GLUT4 intracellular retention
    • Blot V., McGraw T.E. Molecular mechanisms controlling GLUT4 intracellular retention. Mol. Biol. Cell 2008, 19(8):3477-3487.
    • (2008) Mol. Biol. Cell , vol.19 , Issue.8 , pp. 3477-3487
    • Blot, V.1    McGraw, T.E.2
  • 170
    • 0032719409 scopus 로고    scopus 로고
    • Differential regulation of secretory compartments containing the insulin-responsive glucose transporter 4 in 3T3-L1 adipocytes
    • Millar C.A., Shewan A., Hickson G.R., James D.E., Gould G.W. Differential regulation of secretory compartments containing the insulin-responsive glucose transporter 4 in 3T3-L1 adipocytes. Mol. Biol. Cell 1999, 10:3675-3688.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3675-3688
    • Millar, C.A.1    Shewan, A.2    Hickson, G.R.3    James, D.E.4    Gould, G.W.5
  • 171
    • 0034139647 scopus 로고    scopus 로고
    • Adipsin and the glucose transporter GLUT4 traffic to the cell surface via independent pathways in adipocytes
    • Millar C.A., Meerloo T., Martin S., Hickson G.R., Shimwell N.J., Wakelam M.J., et al. Adipsin and the glucose transporter GLUT4 traffic to the cell surface via independent pathways in adipocytes. Traffic 2000, 1:141-151.
    • (2000) Traffic , vol.1 , pp. 141-151
    • Millar, C.A.1    Meerloo, T.2    Martin, S.3    Hickson, G.R.4    Shimwell, N.J.5    Wakelam, M.J.6
  • 173
    • 4644300287 scopus 로고    scopus 로고
    • Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160
    • Zeigerer A., McBrayer M.K., McGraw T.E. Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160. Mol. Biol. Cell 2004, 15:4406-4415.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4406-4415
    • Zeigerer, A.1    McBrayer, M.K.2    McGraw, T.E.3
  • 174
    • 0032031504 scopus 로고    scopus 로고
    • Increased intracellular sequestration of the insulin-regulated aminopeptidase upon differentiation of 3T3-L1 cells
    • Ross S.A., Keller S.R., Lienhard G.E. Increased intracellular sequestration of the insulin-regulated aminopeptidase upon differentiation of 3T3-L1 cells. Biochem. J. 1998, 330:1003-1008.
    • (1998) Biochem. J. , vol.330 , pp. 1003-1008
    • Ross, S.A.1    Keller, S.R.2    Lienhard, G.E.3
  • 175
    • 0023227367 scopus 로고
    • Insulin elicits a redistribution of transferrin receptors in 3T3-L1 adipocytes through an increase in the rate constant for receptor externalization
    • Tanner L.I., Lienhard G.E. Insulin elicits a redistribution of transferrin receptors in 3T3-L1 adipocytes through an increase in the rate constant for receptor externalization. J. Biol. Chem. 1987, 262:8975-8980.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8975-8980
    • Tanner, L.I.1    Lienhard, G.E.2
  • 176
    • 0035206455 scopus 로고    scopus 로고
    • The endosomal compartment is an insulin-sensitive recruitment site for GLUT4 and GLUT1 glucose transporters in cardiac myocytes
    • Becker C., Sevilla L., Tomas E., Palacin M., Zorzano A., Fischer Y. The endosomal compartment is an insulin-sensitive recruitment site for GLUT4 and GLUT1 glucose transporters in cardiac myocytes. Endocrinology 2001, 142:5267-5276.
    • (2001) Endocrinology , vol.142 , pp. 5267-5276
    • Becker, C.1    Sevilla, L.2    Tomas, E.3    Palacin, M.4    Zorzano, A.5    Fischer, Y.6
  • 177
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: insights into insulin action
    • Taniguchi C.M., Emanuelli B., Kahn C.R. Critical nodes in signalling pathways: insights into insulin action. Nat. Rev. Mol. Cell Biol. 2006, 7(2):85-96.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.2 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 178
    • 84874727313 scopus 로고    scopus 로고
    • The insulin receptor: both a prototypical and atypical receptor tyrosine kinase
    • Hubbard S.R. The insulin receptor: both a prototypical and atypical receptor tyrosine kinase. Cold Spring Harb. Perspect. Biol. 2013, 5(3):a008946.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , Issue.3
    • Hubbard, S.R.1
  • 179
    • 0028903554 scopus 로고
    • Requirement for phosphoinositide 3-kinase in insulin-stimulated GLUT4 translocation in 3T3-L1 adipocytes
    • Kotani K., Carozzi A.J., Sakaue H., Hara K., Robinson L.J., Clark S.F., et al. Requirement for phosphoinositide 3-kinase in insulin-stimulated GLUT4 translocation in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 1995, 209:343-348.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 343-348
    • Kotani, K.1    Carozzi, A.J.2    Sakaue, H.3    Hara, K.4    Robinson, L.J.5    Clark, S.F.6
  • 180
    • 0032695529 scopus 로고    scopus 로고
    • A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes
    • Hill M.M., Clark S.F., Tucker D.F., Birnbaum M.J., James D.E., Macaulay S.L. A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes. Mol. Cell Biol. 1999, 19:7771-7781.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 7771-7781
    • Hill, M.M.1    Clark, S.F.2    Tucker, D.F.3    Birnbaum, M.J.4    James, D.E.5    Macaulay, S.L.6
  • 181
    • 62849123090 scopus 로고    scopus 로고
    • ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization
    • Ding J., Du K. ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization. Mol. Cell Biol. 2009, 29(6):1459-1471.
    • (2009) Mol. Cell Biol. , vol.29 , Issue.6 , pp. 1459-1471
    • Ding, J.1    Du, K.2
  • 182
    • 84890284142 scopus 로고    scopus 로고
    • PI3 kinase directly phosphorylates Akt1/2 at Ser473/474 in the insulin signal transduction pathway
    • Tsuchiya A., Kanno T., Nishizaki T. PI3 kinase directly phosphorylates Akt1/2 at Ser473/474 in the insulin signal transduction pathway. J. Endocrinol. 2013, 220(1):49-59.
    • (2013) J. Endocrinol. , vol.220 , Issue.1 , pp. 49-59
    • Tsuchiya, A.1    Kanno, T.2    Nishizaki, T.3
  • 183
    • 84878796897 scopus 로고    scopus 로고
    • Dynamic adipocyte phosphoproteome reveals that Akt directly regulates mTORC2
    • Humphrey S.J., Yang G., Yang P., Fazakerley D.J., Stockli J., Yang J.Y., et al. Dynamic adipocyte phosphoproteome reveals that Akt directly regulates mTORC2. Cell Metab. 2013, 17(6):1009-1020.
    • (2013) Cell Metab. , vol.17 , Issue.6 , pp. 1009-1020
    • Humphrey, S.J.1    Yang, G.2    Yang, P.3    Fazakerley, D.J.4    Stockli, J.5    Yang, J.Y.6
  • 184
    • 0033556016 scopus 로고    scopus 로고
    • Akt-2 binds to GLUT4-containing vesicles and phosphorylates their component proteins in response to insulin
    • Kupriyanova T.A., Kandror K.V. Akt-2 binds to GLUT4-containing vesicles and phosphorylates their component proteins in response to insulin. J. Biol. Chem. 1999, 274:1458-1464.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1458-1464
    • Kupriyanova, T.A.1    Kandror, K.V.2
  • 185
    • 41449087811 scopus 로고    scopus 로고
    • Rapid activation of Akt2 is sufficient to stimulate GLUT4 translocation in 3T3-L1 adipocytes
    • Ng Y., Ramm G., Lopez J.A., James D.E. Rapid activation of Akt2 is sufficient to stimulate GLUT4 translocation in 3T3-L1 adipocytes. Cell Metab. 2008, 7(4):348-356.
    • (2008) Cell Metab. , vol.7 , Issue.4 , pp. 348-356
    • Ng, Y.1    Ramm, G.2    Lopez, J.A.3    James, D.E.4
  • 186
    • 33749489511 scopus 로고    scopus 로고
    • Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane
    • Gonzalez E., McGraw T.E. Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane. Mol. Biol. Cell 2006, 17(10):4484-4493.
    • (2006) Mol. Biol. Cell , vol.17 , Issue.10 , pp. 4484-4493
    • Gonzalez, E.1    McGraw, T.E.2
  • 187
    • 0031724590 scopus 로고    scopus 로고
    • Requirement of atypical protein kinase lambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes
    • Kotani K., Ogawa W., Matsumoto M., Kitamura T., Sakaue H., Hino Y., et al. Requirement of atypical protein kinase lambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes. Mol. Cell Biol. 1998, 18:6971-6982.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6971-6982
    • Kotani, K.1    Ogawa, W.2    Matsumoto, M.3    Kitamura, T.4    Sakaue, H.5    Hino, Y.6
  • 188
    • 0033520373 scopus 로고    scopus 로고
    • Insulin activates protein kinases C-zeta and C-lambda by an autophosphorylation-dependent mechanism and stimulates their translocation to GLUT4 vesicles and other membrane fractions in rat adipocytes
    • Standaert M.L., Bandyopadhyay G., Perez L., Price D., Galloway L., Poklepovic A., et al. Insulin activates protein kinases C-zeta and C-lambda by an autophosphorylation-dependent mechanism and stimulates their translocation to GLUT4 vesicles and other membrane fractions in rat adipocytes. J. Biol. Chem. 1999, 274:25308-25316.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25308-25316
    • Standaert, M.L.1    Bandyopadhyay, G.2    Perez, L.3    Price, D.4    Galloway, L.5    Poklepovic, A.6
  • 189
    • 0034774069 scopus 로고    scopus 로고
    • Activation of protein kinase c-zeta induces serine phosphorylation of VAMP2 in the GLUT4 compartment and increases glucose transport in skeletal muscle
    • Braiman L., Alt A., Kuroki T., Ohba M., Bak A., Tennenbaum T., et al. Activation of protein kinase c-zeta induces serine phosphorylation of VAMP2 in the GLUT4 compartment and increases glucose transport in skeletal muscle. Mol. Cell Biol. 2001, 21:7852-7861.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7852-7861
    • Braiman, L.1    Alt, A.2    Kuroki, T.3    Ohba, M.4    Bak, A.5    Tennenbaum, T.6
  • 190
    • 0033082749 scopus 로고    scopus 로고
    • Effects of transiently expressed atypical (zeta, lambda), conventional (alpha, beta) and novel (delta, epsilon) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-zeta and C-lambda
    • Bandyopadhyay G., Standaert M.L., Kikkawa U., Ono Y., Moscat J., Farese R.V. Effects of transiently expressed atypical (zeta, lambda), conventional (alpha, beta) and novel (delta, epsilon) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-zeta and C-lambda. Biochem. J. 1999, 337(3):461-470.
    • (1999) Biochem. J. , vol.337 , Issue.3 , pp. 461-470
    • Bandyopadhyay, G.1    Standaert, M.L.2    Kikkawa, U.3    Ono, Y.4    Moscat, J.5    Farese, R.V.6
  • 191
    • 23844518719 scopus 로고    scopus 로고
    • Protein kinase-zeta interacts with munc18c: role in GLUT4 trafficking
    • Hodgkinson C.P., Mander A., Sale G.J. Protein kinase-zeta interacts with munc18c: role in GLUT4 trafficking. Diabetologia 2005, 48(8):1627-1636.
    • (2005) Diabetologia , vol.48 , Issue.8 , pp. 1627-1636
    • Hodgkinson, C.P.1    Mander, A.2    Sale, G.J.3
  • 192
    • 0032577464 scopus 로고    scopus 로고
    • Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin
    • Kayali A.G., Eichhorn J., Haruta T., Morris A.J., Nelson J.G., Vollenweider P., et al. Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin. J. Biol. Chem. 1998, 273(22):13808-13818.
    • (1998) J. Biol. Chem. , vol.273 , Issue.22 , pp. 13808-13818
    • Kayali, A.G.1    Eichhorn, J.2    Haruta, T.3    Morris, A.J.4    Nelson, J.G.5    Vollenweider, P.6
  • 193
    • 0030696080 scopus 로고    scopus 로고
    • A role for phospholipase C activity in GLUT4-mediated glucose transport
    • Van Epps-Fung M., Gupta K., Hardy R.W., Wells A. A role for phospholipase C activity in GLUT4-mediated glucose transport. Endocrinology 1997, 138(12):5170-5175.
    • (1997) Endocrinology , vol.138 , Issue.12 , pp. 5170-5175
    • Van Epps-Fung, M.1    Gupta, K.2    Hardy, R.W.3    Wells, A.4
  • 194
    • 0035982104 scopus 로고    scopus 로고
    • PLCgamma participates in insulin stimulation of glucose uptake through activation of PKCzeta in brown adipocytes
    • Lorenzo M., Teruel T., Hernandez R., Kayali A.G., Webster N.J. PLCgamma participates in insulin stimulation of glucose uptake through activation of PKCzeta in brown adipocytes. Exp. Cell Res. 2002, 278(2):146-157.
    • (2002) Exp. Cell Res. , vol.278 , Issue.2 , pp. 146-157
    • Lorenzo, M.1    Teruel, T.2    Hernandez, R.3    Kayali, A.G.4    Webster, N.J.5
  • 195
    • 0035912228 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10
    • Chiang S.H., Baumann C.A., Kanzaki M., Thurmond D.C., Watson R.T., Neudauer C.L., et al. Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10. Nature 2001, 410:944-948.
    • (2001) Nature , vol.410 , pp. 944-948
    • Chiang, S.H.1    Baumann, C.A.2    Kanzaki, M.3    Thurmond, D.C.4    Watson, R.T.5    Neudauer, C.L.6
  • 196
    • 0037431329 scopus 로고    scopus 로고
    • The exocyst complex is required for targeting of GLUT4 to the plasma membrane by insulin
    • Inoue M., Chang L., Hwang J., Chiang S.H., Saltiel A.R. The exocyst complex is required for targeting of GLUT4 to the plasma membrane by insulin. Nature 2003, 422:629-633.
    • (2003) Nature , vol.422 , pp. 629-633
    • Inoue, M.1    Chang, L.2    Hwang, J.3    Chiang, S.H.4    Saltiel, A.R.5
  • 197
    • 67949106616 scopus 로고    scopus 로고
    • The exocyst complex in polarized exocytosis
    • He B., Guo W. The exocyst complex in polarized exocytosis. Curr. Opin. Cell Biol. 2009, 21(4):537-542.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , Issue.4 , pp. 537-542
    • He, B.1    Guo, W.2
  • 198
    • 84862268931 scopus 로고    scopus 로고
    • Exorcising the exocyst complex
    • Heider M.R., Munson M. Exorcising the exocyst complex. Traffic 2012, 13(7):898-907.
    • (2012) Traffic , vol.13 , Issue.7 , pp. 898-907
    • Heider, M.R.1    Munson, M.2
  • 199
    • 33845868011 scopus 로고    scopus 로고
    • TC10alpha is required for insulin-stimulated glucose uptake in adipocytes
    • Chang L., Chiang S.H., Saltiel A.R. TC10alpha is required for insulin-stimulated glucose uptake in adipocytes. Endocrinology 2007, 148(1):27-33.
    • (2007) Endocrinology , vol.148 , Issue.1 , pp. 27-33
    • Chang, L.1    Chiang, S.H.2    Saltiel, A.R.3
  • 200
    • 0036098461 scopus 로고    scopus 로고
    • APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes
    • Liu J., Kimura A., Baumann C.A., Saltiel A.R. APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes. Mol. Cell Biol. 2002, 22(11):3599-3609.
    • (2002) Mol. Cell Biol. , vol.22 , Issue.11 , pp. 3599-3609
    • Liu, J.1    Kimura, A.2    Baumann, C.A.3    Saltiel, A.R.4
  • 201
    • 0031594145 scopus 로고    scopus 로고
    • A novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes
    • Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R. A novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes. Mol. Cell Biol. 1998, 18:872-879.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 872-879
    • Ribon, V.1    Printen, J.A.2    Hoffman, N.G.3    Kay, B.K.4    Saltiel, A.R.5
  • 202
    • 4444228993 scopus 로고    scopus 로고
    • RNAi-based analysis of CAP, Cbl, and CrkII function in the regulation of GLUT4 by insulin
    • Mitra P., Zheng X., Czech M.P. RNAi-based analysis of CAP, Cbl, and CrkII function in the regulation of GLUT4 by insulin. J. Biol. Chem. 2004, 279(36):37431-37435.
    • (2004) J. Biol. Chem. , vol.279 , Issue.36 , pp. 37431-37435
    • Mitra, P.1    Zheng, X.2    Czech, M.P.3
  • 203
    • 65549096355 scopus 로고    scopus 로고
    • Insulin regulates fusion of GLUT4 vesicles independent of Exo70-mediated tethering
    • Lizunov V.A., Lisinski I., Stenkula K., Zimmerberg J., Cushman S.W. Insulin regulates fusion of GLUT4 vesicles independent of Exo70-mediated tethering. J. Biol. Chem. 2009, 284(12):7914-7919.
    • (2009) J. Biol. Chem. , vol.284 , Issue.12 , pp. 7914-7919
    • Lizunov, V.A.1    Lisinski, I.2    Stenkula, K.3    Zimmerberg, J.4    Cushman, S.W.5
  • 204
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance
    • Hotamisligil G.S., Peraldi P., Budavari A., Ellis R., White M.F., Spiegelman B.M. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance. Science 1996, 271(5249):665-668.
    • (1996) Science , vol.271 , Issue.5249 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 205
    • 58149347680 scopus 로고    scopus 로고
    • Muscle-specific IRS-1 Ser->Ala transgenic mice are protected from fat-induced insulin resistance in skeletal muscle
    • Morino K., Neschen S., Bilz S., Sono S., Tsirigotis D., Reznick R.M., et al. Muscle-specific IRS-1 Ser->Ala transgenic mice are protected from fat-induced insulin resistance in skeletal muscle. Diabetes 2008, 57(10):2644-2651.
    • (2008) Diabetes , vol.57 , Issue.10 , pp. 2644-2651
    • Morino, K.1    Neschen, S.2    Bilz, S.3    Sono, S.4    Tsirigotis, D.5    Reznick, R.M.6
  • 206
    • 0035513703 scopus 로고    scopus 로고
    • Ceramide mediates insulin resistance by tumor necrosis factor-alpha in brown adipocytes by maintaining Akt in an inactive dephosphorylated state
    • Teruel T., Hernandez R., Lorenzo M. Ceramide mediates insulin resistance by tumor necrosis factor-alpha in brown adipocytes by maintaining Akt in an inactive dephosphorylated state. Diabetes 2001, 50(11):2563-2571.
    • (2001) Diabetes , vol.50 , Issue.11 , pp. 2563-2571
    • Teruel, T.1    Hernandez, R.2    Lorenzo, M.3
  • 207
    • 84876471343 scopus 로고    scopus 로고
    • Impaired Akt phosphorylation in insulin-resistant human muscle is accompanied by selective and heterogeneous downstream defects
    • Tonks K.T., Ng Y., Miller S., Coster A.C., Samocha-Bonet D., Iseli T.J., et al. Impaired Akt phosphorylation in insulin-resistant human muscle is accompanied by selective and heterogeneous downstream defects. Diabetologia 2013, 56(4):875-885.
    • (2013) Diabetologia , vol.56 , Issue.4 , pp. 875-885
    • Tonks, K.T.1    Ng, Y.2    Miller, S.3    Coster, A.C.4    Samocha-Bonet, D.5    Iseli, T.J.6
  • 208
    • 77949321235 scopus 로고    scopus 로고
    • Dissecting the mechanism of insulin resistance using a novel heterodimerization strategy to activate Akt
    • Ng Y., Ramm G., James D.E. Dissecting the mechanism of insulin resistance using a novel heterodimerization strategy to activate Akt. J. Biol. Chem. 2010, 285(8):5232-5239.
    • (2010) J. Biol. Chem. , vol.285 , Issue.8 , pp. 5232-5239
    • Ng, Y.1    Ramm, G.2    James, D.E.3
  • 209
    • 33644634452 scopus 로고    scopus 로고
    • Activation of the Cbl insulin signaling pathway in cardiac muscle dysregulation in obesity and diabetes
    • Gupte A., Mora S. Activation of the Cbl insulin signaling pathway in cardiac muscle dysregulation in obesity and diabetes. Biochem. Biophys. Res. Commun. 2006, 342(3):751-757.
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , Issue.3 , pp. 751-757
    • Gupte, A.1    Mora, S.2
  • 210
    • 44449115735 scopus 로고    scopus 로고
    • High-fat diet alters PP2A, TC10, and CIP4 expression in visceral adipose tissue of rats
    • Jun H.S., Hwang K., Kim Y., Park T. High-fat diet alters PP2A, TC10, and CIP4 expression in visceral adipose tissue of rats. Obesity 2008, 16(6):1226-1231.
    • (2008) Obesity , vol.16 , Issue.6 , pp. 1226-1231
    • Jun, H.S.1    Hwang, K.2    Kim, Y.3    Park, T.4
  • 211
    • 0037151026 scopus 로고    scopus 로고
    • A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain
    • Kane S., Sano H., Liu S.C., Asara J.M., Lane W.S., Garner C.C., et al. A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain. J. Biol. Chem. 2002, 277:22115-22118.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22115-22118
    • Kane, S.1    Sano, H.2    Liu, S.C.3    Asara, J.M.4    Lane, W.S.5    Garner, C.C.6
  • 212
    • 84869195388 scopus 로고    scopus 로고
    • Deletion of Rab GAP AS160 modifies glucose uptake and GLUT4 translocation in primary skeletal muscles and adipocytes and impairs glucose homeostasis
    • Lansey M.N., Walker N.N., Hargett S.R., Stevens J.R., Keller S.R. Deletion of Rab GAP AS160 modifies glucose uptake and GLUT4 translocation in primary skeletal muscles and adipocytes and impairs glucose homeostasis. Am. J. Physiol. Endocrinol. Metab. 2012, 303(10):E1273-E1286.
    • (2012) Am. J. Physiol. Endocrinol. Metab. , vol.303 , Issue.10
    • Lansey, M.N.1    Walker, N.N.2    Hargett, S.R.3    Stevens, J.R.4    Keller, S.R.5
  • 213
    • 26844573782 scopus 로고    scopus 로고
    • AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain
    • Miinea C.P., Sano H., Kane S., Sano E., Fukuda M., Peranen J., et al. AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain. Biochem. J. 2005, 391(1):87-93.
    • (2005) Biochem. J. , vol.391 , Issue.1 , pp. 87-93
    • Miinea, C.P.1    Sano, H.2    Kane, S.3    Sano, E.4    Fukuda, M.5    Peranen, J.6
  • 214
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S., et al. Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J. Biol. Chem. 2003, 278:14599-14602.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3    Miinea, C.P.4    Asara, J.M.5    Lane, W.S.6
  • 215
    • 84864573006 scopus 로고    scopus 로고
    • The association of ClipR-59 protein with AS160 modulates AS160 protein phosphorylation and adipocyte GLUT4 protein membrane translocation
    • Ren W., Cheema S., Du K. The association of ClipR-59 protein with AS160 modulates AS160 protein phosphorylation and adipocyte GLUT4 protein membrane translocation. J. Biol. Chem. 2012, 287(32):26890-26900.
    • (2012) J. Biol. Chem. , vol.287 , Issue.32 , pp. 26890-26900
    • Ren, W.1    Cheema, S.2    Du, K.3
  • 216
    • 77449115115 scopus 로고    scopus 로고
    • Cluster analysis of insulin action in adipocytes reveals a key role for Akt at the plasma membrane
    • Ng Y., Ramm G., Burchfield J.G., Coster A.C., Stockli J., James D.E. Cluster analysis of insulin action in adipocytes reveals a key role for Akt at the plasma membrane. J. Biol. Chem. 2010, 285(4):2245-2257.
    • (2010) J. Biol. Chem. , vol.285 , Issue.4 , pp. 2245-2257
    • Ng, Y.1    Ramm, G.2    Burchfield, J.G.3    Coster, A.C.4    Stockli, J.5    James, D.E.6
  • 217
    • 56749173518 scopus 로고    scopus 로고
    • Regulation of glucose transporter 4 translocation by the Rab guanosine triphosphatase-activating protein AS160/TBC1D4: role of phosphorylation and membrane association
    • Stockli J., Davey J.R., Hohnen-Behrens C., Xu A., James D.E., Ramm G. Regulation of glucose transporter 4 translocation by the Rab guanosine triphosphatase-activating protein AS160/TBC1D4: role of phosphorylation and membrane association. Mol. Endocrinol. 2008, 22(12):2703-2715.
    • (2008) Mol. Endocrinol. , vol.22 , Issue.12 , pp. 2703-2715
    • Stockli, J.1    Davey, J.R.2    Hohnen-Behrens, C.3    Xu, A.4    James, D.E.5    Ramm, G.6
  • 218
    • 78650897555 scopus 로고    scopus 로고
    • Mice with AS160/TBC1D4-Thr649Ala knockin mutation are glucose intolerant with reduced insulin sensitivity and altered GLUT4 trafficking
    • Chen S., Wasserman D.H., MacKintosh C., Sakamoto K. Mice with AS160/TBC1D4-Thr649Ala knockin mutation are glucose intolerant with reduced insulin sensitivity and altered GLUT4 trafficking. Cell Metab. 2011, 13(1):68-79.
    • (2011) Cell Metab. , vol.13 , Issue.1 , pp. 68-79
    • Chen, S.1    Wasserman, D.H.2    MacKintosh, C.3    Sakamoto, K.4
  • 219
    • 33847062845 scopus 로고    scopus 로고
    • The Rab GTPase-activating protein AS160 integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulating GLUT4 traffic
    • Thong F.S., Bilan P.J., Klip A. The Rab GTPase-activating protein AS160 integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulating GLUT4 traffic. Diabetes 2007, 56(2):414-423.
    • (2007) Diabetes , vol.56 , Issue.2 , pp. 414-423
    • Thong, F.S.1    Bilan, P.J.2    Klip, A.3
  • 220
    • 28544435205 scopus 로고    scopus 로고
    • Full intracellular retention of GLUT4 requires AS160 Rab GTPase activating protein
    • Eguez L., Lee A., Chavez J.A., Miinea C.P., Kane S., Lienhard G.E., et al. Full intracellular retention of GLUT4 requires AS160 Rab GTPase activating protein. Cell Metab. 2005, 2(4):263-272.
    • (2005) Cell Metab. , vol.2 , Issue.4 , pp. 263-272
    • Eguez, L.1    Lee, A.2    Chavez, J.A.3    Miinea, C.P.4    Kane, S.5    Lienhard, G.E.6
  • 221
    • 57049184703 scopus 로고    scopus 로고
    • Muscle cells engage Rab8A and myosin Vb in insulin-dependent GLUT4 translocation
    • Ishikura S., Klip A. Muscle cells engage Rab8A and myosin Vb in insulin-dependent GLUT4 translocation. Am. J. Physiol. Cell Physiol. 2008, 295(4):C1016-C1025.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295 , Issue.4
    • Ishikura, S.1    Klip, A.2
  • 222
    • 79960665062 scopus 로고    scopus 로고
    • Loss of AS160 Akt substrate causes GLUT4 protein to accumulate in compartments that are primed for fusion in basal adipocytes
    • Brewer P.D., Romenskaia I., Kanow M.A., Mastick C.C. Loss of AS160 Akt substrate causes GLUT4 protein to accumulate in compartments that are primed for fusion in basal adipocytes. J. Biol. Chem. 2011, 286(30):26287-26297.
    • (2011) J. Biol. Chem. , vol.286 , Issue.30 , pp. 26287-26297
    • Brewer, P.D.1    Romenskaia, I.2    Kanow, M.A.3    Mastick, C.C.4
  • 223
    • 84882762459 scopus 로고    scopus 로고
    • Specialized sorting of GLUT4 and its recruitment to the cell surface are independently regulated by distinct Rabs
    • Sadacca L.A., Bruno J., Wen J., Xiong W., McGraw T.E. Specialized sorting of GLUT4 and its recruitment to the cell surface are independently regulated by distinct Rabs. Mol. Biol. Cell 2013, 24(16):2544-2557.
    • (2013) Mol. Biol. Cell , vol.24 , Issue.16 , pp. 2544-2557
    • Sadacca, L.A.1    Bruno, J.2    Wen, J.3    Xiong, W.4    McGraw, T.E.5
  • 224
    • 43749096120 scopus 로고    scopus 로고
    • Direct quantification of fusion rate reveals a distal role for AS160 in insulin-stimulated fusion of GLUT4 storage vesicles
    • Jiang L., Fan J., Bai L., Wang Y., Chen Y., Yang L., et al. Direct quantification of fusion rate reveals a distal role for AS160 in insulin-stimulated fusion of GLUT4 storage vesicles. J. Biol. Chem. 2008, 283(13):8508-8516.
    • (2008) J. Biol. Chem. , vol.283 , Issue.13 , pp. 8508-8516
    • Jiang, L.1    Fan, J.2    Bai, L.3    Wang, Y.4    Chen, Y.5    Yang, L.6
  • 225
    • 33845666593 scopus 로고    scopus 로고
    • Dissecting multiple steps of GLUT4 trafficking and identifying the sites of insulin action
    • Bai L., Wang Y., Fan J., Chen Y., Ji W., Qu A., et al. Dissecting multiple steps of GLUT4 trafficking and identifying the sites of insulin action. Cell Metab. 2007, 5(1):47-57.
    • (2007) Cell Metab. , vol.5 , Issue.1 , pp. 47-57
    • Bai, L.1    Wang, Y.2    Fan, J.3    Chen, Y.4    Ji, W.5    Qu, A.6
  • 226
    • 77955123564 scopus 로고    scopus 로고
    • Identification of three distinct functional sites of insulin-mediated GLUT4 trafficking in adipocytes using quantitative single molecule imaging
    • Fujita H., Hatakeyama H., Watanabe T.M., Sato M., Higuchi H., Kanzaki M. Identification of three distinct functional sites of insulin-mediated GLUT4 trafficking in adipocytes using quantitative single molecule imaging. Mol. Biol. Cell 2010, 21(15):2721-2731.
    • (2010) Mol. Biol. Cell , vol.21 , Issue.15 , pp. 2721-2731
    • Fujita, H.1    Hatakeyama, H.2    Watanabe, T.M.3    Sato, M.4    Higuchi, H.5    Kanzaki, M.6
  • 227
    • 55249098126 scopus 로고    scopus 로고
    • GLUT4 vesicle recruitment and fusion are differentially regulated by Rac, AS160, and Rab8A in muscle cells
    • Randhawa V.K., Ishikura S., Talior-Volodarsky I., Cheng A.W., Patel N., Hartwig J.H., et al. GLUT4 vesicle recruitment and fusion are differentially regulated by Rac, AS160, and Rab8A in muscle cells. J. Biol. Chem. 2008, 283(40):27208-27219.
    • (2008) J. Biol. Chem. , vol.283 , Issue.40 , pp. 27208-27219
    • Randhawa, V.K.1    Ishikura, S.2    Talior-Volodarsky, I.3    Cheng, A.W.4    Patel, N.5    Hartwig, J.H.6
  • 228
    • 84871902200 scopus 로고    scopus 로고
    • The Rab GTPase-activating protein TBC1D4/AS160 contains an atypical phosphotyrosine-binding domain that interacts with plasma membrane phospholipids to facilitate GLUT4 trafficking in adipocytes
    • Tan S.X., Ng Y., Burchfield J.G., Ramm G., Lambright D.G., Stockli J., et al. The Rab GTPase-activating protein TBC1D4/AS160 contains an atypical phosphotyrosine-binding domain that interacts with plasma membrane phospholipids to facilitate GLUT4 trafficking in adipocytes. Mol. Cell Biol. 2012, 32(24):4946-4959.
    • (2012) Mol. Cell Biol. , vol.32 , Issue.24 , pp. 4946-4959
    • Tan, S.X.1    Ng, Y.2    Burchfield, J.G.3    Ramm, G.4    Lambright, D.G.5    Stockli, J.6
  • 229
    • 80052770295 scopus 로고    scopus 로고
    • C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane
    • Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., et al. C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane. Cell Metab. 2011, 14(3):378-389.
    • (2011) Cell Metab. , vol.14 , Issue.3 , pp. 378-389
    • Xie, X.1    Gong, Z.2    Mansuy-Aubert, V.3    Zhou, Q.L.4    Tatulian, S.A.5    Sehrt, D.6
  • 230
    • 0033153025 scopus 로고    scopus 로고
    • Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes
    • Min J., Okada S., Kanzaki M., Elmendorf J.S., Coker K.J., Ceresa B.P., et al. Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes. Mol. Cell 1999, 3:751-760.
    • (1999) Mol. Cell , vol.3 , pp. 751-760
    • Min, J.1    Okada, S.2    Kanzaki, M.3    Elmendorf, J.S.4    Coker, K.J.5    Ceresa, B.P.6
  • 231
    • 15444374951 scopus 로고    scopus 로고
    • Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles
    • Yamada E., Okada S., Saito T., Ohshima K., Sato M., Tsuchiya T., et al. Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles. J. Cell Biol. 2005, 168(6):921-928.
    • (2005) J. Cell Biol. , vol.168 , Issue.6 , pp. 921-928
    • Yamada, E.1    Okada, S.2    Saito, T.3    Ohshima, K.4    Sato, M.5    Tsuchiya, T.6
  • 233
    • 19744378802 scopus 로고    scopus 로고
    • Synip phosphorylation does not regulate insulin-stimulated GLUT4 translocation
    • Sano H., Kane S., Sano E., Lienhard G.E. Synip phosphorylation does not regulate insulin-stimulated GLUT4 translocation. Biochem. Biophys. Res. Commun. 2005, 332(3):880-884.
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , Issue.3 , pp. 880-884
    • Sano, H.1    Kane, S.2    Sano, E.3    Lienhard, G.E.4
  • 234
    • 34447499043 scopus 로고    scopus 로고
    • Myosin 5a is an insulin-stimulated Akt2 (protein kinase B beta) substrate modulating GLUT4 vesicle translocation
    • Yoshizaki T., Imamura T., Babendure J.L., Lu J.C., Sonoda N., Olefsky J.M. Myosin 5a is an insulin-stimulated Akt2 (protein kinase B beta) substrate modulating GLUT4 vesicle translocation. Mol. Cell Biol. 2007, 27(14):5172-5183.
    • (2007) Mol. Cell Biol. , vol.27 , Issue.14 , pp. 5172-5183
    • Yoshizaki, T.1    Imamura, T.2    Babendure, J.L.3    Lu, J.C.4    Sonoda, N.5    Olefsky, J.M.6
  • 235
    • 84862119644 scopus 로고    scopus 로고
    • Grp1 plays a key role in linking insulin signaling to GLUT4 recycling
    • Li J., Malaby A.W., Famulok M., Sabe H., Lambright D.G., Hsu V.W. Grp1 plays a key role in linking insulin signaling to GLUT4 recycling. Dev. Cell 2012, 22(6):1286-1298.
    • (2012) Dev. Cell , vol.22 , Issue.6 , pp. 1286-1298
    • Li, J.1    Malaby, A.W.2    Famulok, M.3    Sabe, H.4    Lambright, D.G.5    Hsu, V.W.6
  • 236
    • 0033580823 scopus 로고    scopus 로고
    • Evidence for a role for ADP-ribosylation factor 6 in insulin-stimulated glucose transporter-4 (GLUT4) trafficking in 3T3-L1 adipocytes
    • Millar C.A., Powell K.A., Hickson G.R., Bader M.F., Gould G.W. Evidence for a role for ADP-ribosylation factor 6 in insulin-stimulated glucose transporter-4 (GLUT4) trafficking in 3T3-L1 adipocytes. J. Biol. Chem. 1999, 274:17619-17625.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17619-17625
    • Millar, C.A.1    Powell, K.A.2    Hickson, G.R.3    Bader, M.F.4    Gould, G.W.5
  • 237
    • 12344290720 scopus 로고    scopus 로고
    • Protein kinase B phosphorylation of PIKfyve regulates the trafficking of GLUT4 vesicles
    • Berwick D.C., Dell G.C., Welsh G.I., Heesom K.J., Hers I., Fletcher L.M., et al. Protein kinase B phosphorylation of PIKfyve regulates the trafficking of GLUT4 vesicles. J. Cell Sci. 2004, 117(25):5985-5993.
    • (2004) J. Cell Sci. , vol.117 , Issue.25 , pp. 5985-5993
    • Berwick, D.C.1    Dell, G.C.2    Welsh, G.I.3    Heesom, K.J.4    Hers, I.5    Fletcher, L.M.6
  • 239
    • 34250006277 scopus 로고    scopus 로고
    • ArPIKfyve-PIKfyve interaction and role in insulin-regulated GLUT4 translocation and glucose transport in 3T3-L1 adipocytes
    • Ikonomov O.C., Sbrissa D., Dondapati R., Shisheva A. ArPIKfyve-PIKfyve interaction and role in insulin-regulated GLUT4 translocation and glucose transport in 3T3-L1 adipocytes. Exp. Cell Res. 2007, 313(11):2404-2416.
    • (2007) Exp. Cell Res. , vol.313 , Issue.11 , pp. 2404-2416
    • Ikonomov, O.C.1    Sbrissa, D.2    Dondapati, R.3    Shisheva, A.4
  • 240
    • 84879559972 scopus 로고    scopus 로고
    • Muscle-specific Pikfyve gene disruption causes glucose intolerance, insulin resistance, adiposity, and hyperinsulinemia but not muscle fiber-type switching
    • Ikonomov O.C., Sbrissa D., Delvecchio K., Feng H.Z., Cartee G.D., Jin J.P., et al. Muscle-specific Pikfyve gene disruption causes glucose intolerance, insulin resistance, adiposity, and hyperinsulinemia but not muscle fiber-type switching. Am. J. Physiol. Endocrinol. Metab. 2013, 305(1):E119-E131.
    • (2013) Am. J. Physiol. Endocrinol. Metab. , vol.305 , Issue.1
    • Ikonomov, O.C.1    Sbrissa, D.2    Delvecchio, K.3    Feng, H.Z.4    Cartee, G.D.5    Jin, J.P.6
  • 241
    • 0034435239 scopus 로고    scopus 로고
    • Rab11 is associated with GLUT4-containing vesicles and redistributes in response to insulin
    • Kessler A., Tomas E., Immler D., Meyer H.E., Zorzano A., Eckel J. Rab11 is associated with GLUT4-containing vesicles and redistributes in response to insulin. Diabetologia 2000, 43:1518-1527.
    • (2000) Diabetologia , vol.43 , pp. 1518-1527
    • Kessler, A.1    Tomas, E.2    Immler, D.3    Meyer, H.E.4    Zorzano, A.5    Eckel, J.6
  • 242
    • 33947578085 scopus 로고    scopus 로고
    • Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane
    • Sano H., Eguez L., Teruel M.N., Fukuda M., Chuang T.D., Chavez J.A., et al. Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane. Cell Metab. 2007, 5(4):293-303.
    • (2007) Cell Metab. , vol.5 , Issue.4 , pp. 293-303
    • Sano, H.1    Eguez, L.2    Teruel, M.N.3    Fukuda, M.4    Chuang, T.D.5    Chavez, J.A.6
  • 244
    • 79955766872 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 protein translocation in adipocytes requires the Rab10 guanine nucleotide exchange factor Dennd4C
    • Sano H., Peck G.R., Kettenbach A.N., Gerber S.A., Lienhard G.E. Insulin-stimulated GLUT4 protein translocation in adipocytes requires the Rab10 guanine nucleotide exchange factor Dennd4C. J. Biol. Chem. 2011, 286(19):16541-16545.
    • (2011) J. Biol. Chem. , vol.286 , Issue.19 , pp. 16541-16545
    • Sano, H.1    Peck, G.R.2    Kettenbach, A.N.3    Gerber, S.A.4    Lienhard, G.E.5
  • 245
    • 84878666414 scopus 로고    scopus 로고
    • A role for Rab14 in the endocytic trafficking of GLUT4 in 3T3-L1 adipocytes
    • Reed S.E., Hodgson L.R., Song S., May M.T., Kelly E.E., McCaffrey M.W., et al. A role for Rab14 in the endocytic trafficking of GLUT4 in 3T3-L1 adipocytes. J. Cell Sci. 2013, 126(9):1931-1941.
    • (2013) J. Cell Sci. , vol.126 , Issue.9 , pp. 1931-1941
    • Reed, S.E.1    Hodgson, L.R.2    Song, S.3    May, M.T.4    Kelly, E.E.5    McCaffrey, M.W.6
  • 246
    • 0035818483 scopus 로고    scopus 로고
    • Insulin can regulate GLUT4 internalization by signaling to Rab5 and the motor protein dynein
    • Huang J., Imamura T., Olefsky J.M. Insulin can regulate GLUT4 internalization by signaling to Rab5 and the motor protein dynein. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:13084-13089.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13084-13089
    • Huang, J.1    Imamura, T.2    Olefsky, J.M.3
  • 247
    • 33845572827 scopus 로고    scopus 로고
    • Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates GLUT4 trafficking in adipocytes
    • Lodhi I.J., Chiang S.H., Chang L., Vollenweider D., Watson R.T., Inoue M., et al. Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates GLUT4 trafficking in adipocytes. Cell Metab. 2007, 5(1):59-72.
    • (2007) Cell Metab. , vol.5 , Issue.1 , pp. 59-72
    • Lodhi, I.J.1    Chiang, S.H.2    Chang, L.3    Vollenweider, D.4    Watson, R.T.5    Inoue, M.6
  • 248
    • 0035969243 scopus 로고    scopus 로고
    • Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells
    • Yeaman C., Grindstaff K.K., Wright J.R., Nelson W.J. Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells. J. Cell Biol. 2001, 155:593-604.
    • (2001) J. Cell Biol. , vol.155 , pp. 593-604
    • Yeaman, C.1    Grindstaff, K.K.2    Wright, J.R.3    Nelson, W.J.4
  • 249
    • 38349011116 scopus 로고    scopus 로고
    • Rip11 is a Rab11- and AS160-RabGAP-binding protein required for insulin-stimulated glucose uptake in adipocytes
    • Welsh G.I., Leney S.E., Lloyd-Lewis B., Wherlock M., Lindsay A.J., McCaffrey M.W., et al. Rip11 is a Rab11- and AS160-RabGAP-binding protein required for insulin-stimulated glucose uptake in adipocytes. J. Cell Sci. 2007, 120(23):4197-4208.
    • (2007) J. Cell Sci. , vol.120 , Issue.23 , pp. 4197-4208
    • Welsh, G.I.1    Leney, S.E.2    Lloyd-Lewis, B.3    Wherlock, M.4    Lindsay, A.J.5    McCaffrey, M.W.6
  • 251
    • 0038451252 scopus 로고    scopus 로고
    • Insulin-induced GLUT4 translocation involves protein kinase C-lambda-mediated functional coupling between Rab4 and the motor protein kinesin
    • Imamura T., Huang J., Usui I., Satoh H., Bever J., Olefsky J.M. Insulin-induced GLUT4 translocation involves protein kinase C-lambda-mediated functional coupling between Rab4 and the motor protein kinesin. Mol. Cell Biol. 2003, 23:4892-4900.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4892-4900
    • Imamura, T.1    Huang, J.2    Usui, I.3    Satoh, H.4    Bever, J.5    Olefsky, J.M.6
  • 252
    • 77749306186 scopus 로고    scopus 로고
    • Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4
    • Jewell J.L., Oh E., Thurmond D.C. Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2010, 298(3):R517-R531.
    • (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.298 , Issue.3
    • Jewell, J.L.1    Oh, E.2    Thurmond, D.C.3
  • 253
  • 254
    • 0030917678 scopus 로고    scopus 로고
    • Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation
    • Macaulay S.L., Hewish D.R., Gough K.H., Stoichevska V., MacPherson S.F., Jagadish M., et al. Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation. Biochem. J. 1997, 324:217-224.
    • (1997) Biochem. J. , vol.324 , pp. 217-224
    • Macaulay, S.L.1    Hewish, D.R.2    Gough, K.H.3    Stoichevska, V.4    MacPherson, S.F.5    Jagadish, M.6
  • 255
    • 0031891004 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes
    • Martin L.B., Shewan A., Millar C.A., Gould G.W., James D.E. Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes. J. Biol. Chem. 1998, 273:1444-1452.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1444-1452
    • Martin, L.B.1    Shewan, A.2    Millar, C.A.3    Gould, G.W.4    James, D.E.5
  • 256
    • 0029992462 scopus 로고    scopus 로고
    • Cleavage of vesicle-associated membrane protein (VAMP)-2 and cellubrevin on GLUT4-containing vesicles inhibits the translocation of GLUT4 in 3T3-L1 adipocytes
    • Tamori Y., Hashiramoto M., Araki S., Kamata Y., Takahashi M., Kozaki S., et al. Cleavage of vesicle-associated membrane protein (VAMP)-2 and cellubrevin on GLUT4-containing vesicles inhibits the translocation of GLUT4 in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 1996, 220:740-745.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 740-745
    • Tamori, Y.1    Hashiramoto, M.2    Araki, S.3    Kamata, Y.4    Takahashi, M.5    Kozaki, S.6
  • 257
    • 0029853689 scopus 로고    scopus 로고
    • Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein
    • Timmers K.I., Clark A.E., Omatsu-Kanbe M., Whiteheart S.W., Bennett M.K., Holman G.D., et al. Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein. Biochem. J. 1996, 320:429-436.
    • (1996) Biochem. J. , vol.320 , pp. 429-436
    • Timmers, K.I.1    Clark, A.E.2    Omatsu-Kanbe, M.3    Whiteheart, S.W.4    Bennett, M.K.5    Holman, G.D.6
  • 258
    • 84876565914 scopus 로고    scopus 로고
    • Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending-dependent manner
    • Yu H., Rathore S.S., Davis E.M., Ouyang Y., Shen J. Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending-dependent manner. Mol. Biol. Cell 2013, 24(8):1176-1184.
    • (2013) Mol. Biol. Cell , vol.24 , Issue.8 , pp. 1176-1184
    • Yu, H.1    Rathore, S.S.2    Davis, E.M.3    Ouyang, Y.4    Shen, J.5
  • 259
    • 0031023409 scopus 로고    scopus 로고
    • Proteolytic cleavage of cellubrevin and vesicle-associated membrane protein (VAMP) by tetanus toxin does not impair insulin-stimulated glucose transport or GLUT4 translocation in rat adipocytes
    • Hajduch E., Aledo J.C., Watts C., Hundal H.S. Proteolytic cleavage of cellubrevin and vesicle-associated membrane protein (VAMP) by tetanus toxin does not impair insulin-stimulated glucose transport or GLUT4 translocation in rat adipocytes. Biochem. J. 1997, 321(1):233-238.
    • (1997) Biochem. J. , vol.321 , Issue.1 , pp. 233-238
    • Hajduch, E.1    Aledo, J.C.2    Watts, C.3    Hundal, H.S.4
  • 260
    • 0033215390 scopus 로고    scopus 로고
    • Protein kinase B stimulates the translocation of GLUT4 but not GLUT1 or transferrin receptors in 3T3-L1 adipocytes by a pathway involving SNAP-23, synaptobrevin-2, and/or cellubrevin
    • Foran P.G., Fletcher L.M., Oatey P.B., Mohammed N., Dolly J.O., Tavare J.M. Protein kinase B stimulates the translocation of GLUT4 but not GLUT1 or transferrin receptors in 3T3-L1 adipocytes by a pathway involving SNAP-23, synaptobrevin-2, and/or cellubrevin. J. Biol. Chem. 1999, 274:28087-28095.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28087-28095
    • Foran, P.G.1    Fletcher, L.M.2    Oatey, P.B.3    Mohammed, N.4    Dolly, J.O.5    Tavare, J.M.6
  • 261
    • 0030937422 scopus 로고    scopus 로고
    • Syntaxin 4, VAMP2, and/or VAMP3/cellubrevin are functional target membrane and vesicle SNAP receptors for insulin-stimulated GLUT4 translocation in adipocytes
    • Olson A.L., Knight J.B., Pessin J.E. Syntaxin 4, VAMP2, and/or VAMP3/cellubrevin are functional target membrane and vesicle SNAP receptors for insulin-stimulated GLUT4 translocation in adipocytes. Mol. Cell Biol. 1997, 17:2425-2435.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2425-2435
    • Olson, A.L.1    Knight, J.B.2    Pessin, J.E.3
  • 262
    • 0033915755 scopus 로고    scopus 로고
    • VAMP2, but not VAMP3/cellubrevin, mediates insulin-dependent incorporation of GLUT4 into the plasma membrane of L6 myoblasts
    • Randhawa V.K., Bilan P.J., Khayat Z.A., Daneman N., Liu Z., Ramlal T., et al. VAMP2, but not VAMP3/cellubrevin, mediates insulin-dependent incorporation of GLUT4 into the plasma membrane of L6 myoblasts. Mol. Biol. Cell 2000, 11:2403-2417.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2403-2417
    • Randhawa, V.K.1    Bilan, P.J.2    Khayat, Z.A.3    Daneman, N.4    Liu, Z.5    Ramlal, T.6
  • 263
    • 38749105050 scopus 로고    scopus 로고
    • Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes
    • Williams D., Pessin J.E. Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes. J. Cell Biol. 2008, 180(2):375-387.
    • (2008) J. Cell Biol. , vol.180 , Issue.2 , pp. 375-387
    • Williams, D.1    Pessin, J.E.2
  • 264
    • 27144539525 scopus 로고    scopus 로고
    • Trans-Golgi network syntaxin 10 functions distinctly from syntaxins 6 and 16
    • Wang Y., Tai G., Lu L., Johannes L., Hong W., Tang B.L. Trans-Golgi network syntaxin 10 functions distinctly from syntaxins 6 and 16. Mol. Membr. Biol. 2005, 22(4):313-325.
    • (2005) Mol. Membr. Biol. , vol.22 , Issue.4 , pp. 313-325
    • Wang, Y.1    Tai, G.2    Lu, L.3    Johannes, L.4    Hong, W.5    Tang, B.L.6
  • 265
    • 84881061444 scopus 로고    scopus 로고
    • Sorting of GLUT4 into its insulin-sensitive store requires the Sec1/Munc18 protein mVps45
    • Roccisana J., Sadler J.B., Bryant N.J., Gould G.W. Sorting of GLUT4 into its insulin-sensitive store requires the Sec1/Munc18 protein mVps45. Mol. Biol. Cell 2013, 24(15):2389-2397.
    • (2013) Mol. Biol. Cell , vol.24 , Issue.15 , pp. 2389-2397
    • Roccisana, J.1    Sadler, J.B.2    Bryant, N.J.3    Gould, G.W.4
  • 266
    • 0032538835 scopus 로고    scopus 로고
    • Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes
    • Prekeris R., Klumperman J., Chen Y.A., Scheller R.H. Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. J. Cell Biol. 1998, 143(4):957-971.
    • (1998) J. Cell Biol. , vol.143 , Issue.4 , pp. 957-971
    • Prekeris, R.1    Klumperman, J.2    Chen, Y.A.3    Scheller, R.H.4
  • 267
    • 33745758070 scopus 로고    scopus 로고
    • A second SNARE role for exocytic SNAP25 in endosome fusion
    • Aikawa Y., Lynch K.L., Boswell K.L., Martin T.F. A second SNARE role for exocytic SNAP25 in endosome fusion. Mol. Biol. Cell 2006, 17(5):2113-2124.
    • (2006) Mol. Biol. Cell , vol.17 , Issue.5 , pp. 2113-2124
    • Aikawa, Y.1    Lynch, K.L.2    Boswell, K.L.3    Martin, T.F.4
  • 268
    • 0032584609 scopus 로고    scopus 로고
    • Inhibition of insulin-induced GLUT4 translocation by Munc18c through interaction with syntaxin4 in 3T3-L1 adipocytes
    • Tamori Y., Kawanishi M., Niki T., Shinoda H., Araki S., Okazawa H., et al. Inhibition of insulin-induced GLUT4 translocation by Munc18c through interaction with syntaxin4 in 3T3-L1 adipocytes. J. Biol. Chem. 1998, 273:19740-19746.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19740-19746
    • Tamori, Y.1    Kawanishi, M.2    Niki, T.3    Shinoda, H.4    Araki, S.5    Okazawa, H.6
  • 270
    • 0037174130 scopus 로고    scopus 로고
    • Cellular munc18c levels can modulate glucose transport rate and GLUT4 translocation in 3T3L1 cells
    • Macaulay S., Grusovin J., Stoichevska V., Ryan J., Castelli L., Ward C. Cellular munc18c levels can modulate glucose transport rate and GLUT4 translocation in 3T3L1 cells. FEBS Lett. 2002, 528:154.
    • (2002) FEBS Lett. , vol.528 , pp. 154
    • Macaulay, S.1    Grusovin, J.2    Stoichevska, V.3    Ryan, J.4    Castelli, L.5    Ward, C.6
  • 271
    • 34447543968 scopus 로고    scopus 로고
    • Munc18c interaction with syntaxin 4 monomers and SNARE complex intermediates in GLUT4 vesicle trafficking
    • D'Andrea-Merrins M., Chang L., Lam A.D., Ernst S.A., Stuenkel E.L. Munc18c interaction with syntaxin 4 monomers and SNARE complex intermediates in GLUT4 vesicle trafficking. J. Biol. Chem. 2007, 282(22):16553-16566.
    • (2007) J. Biol. Chem. , vol.282 , Issue.22 , pp. 16553-16566
    • D'Andrea-Merrins, M.1    Chang, L.2    Lam, A.D.3    Ernst, S.A.4    Stuenkel, E.L.5
  • 272
    • 33749332751 scopus 로고    scopus 로고
    • Temporal dynamics of tyrosine phosphorylation in insulin signaling
    • Schmelzle K., Kane S., Gridley S., Lienhard G.E., White F.M. Temporal dynamics of tyrosine phosphorylation in insulin signaling. Diabetes 2006, 55(8):2171-2179.
    • (2006) Diabetes , vol.55 , Issue.8 , pp. 2171-2179
    • Schmelzle, K.1    Kane, S.2    Gridley, S.3    Lienhard, G.E.4    White, F.M.5
  • 273
    • 79955517215 scopus 로고    scopus 로고
    • Munc18c phosphorylation by the insulin receptor links cell signaling directly to SNARE exocytosis
    • Jewell J.L., Oh E., Ramalingam L., Kalwat M.A., Tagliabracci V.S., Tackett L., et al. Munc18c phosphorylation by the insulin receptor links cell signaling directly to SNARE exocytosis. J. Cell Biol. 2011, 193(1):185-199.
    • (2011) J. Cell Biol. , vol.193 , Issue.1 , pp. 185-199
    • Jewell, J.L.1    Oh, E.2    Ramalingam, L.3    Kalwat, M.A.4    Tagliabracci, V.S.5    Tackett, L.6
  • 274
    • 33745834309 scopus 로고    scopus 로고
    • The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis
    • Oh E., Thurmond D.C. The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis. J. Biol. Chem. 2006, 281(26):17624-17634.
    • (2006) J. Biol. Chem. , vol.281 , Issue.26 , pp. 17624-17634
    • Oh, E.1    Thurmond, D.C.2
  • 275
    • 40449092630 scopus 로고    scopus 로고
    • Insulin-triggered repositioning of munc18c on syntaxin-4 in GLUT4 signalling
    • Smithers N.P., Hodgkinson C.P., Cuttle M., Sale G.J. Insulin-triggered repositioning of munc18c on syntaxin-4 in GLUT4 signalling. Biochem. J. 2008, 410(2):255-260.
    • (2008) Biochem. J. , vol.410 , Issue.2 , pp. 255-260
    • Smithers, N.P.1    Hodgkinson, C.P.2    Cuttle, M.3    Sale, G.J.4
  • 276
    • 85047691831 scopus 로고    scopus 로고
    • Adipocytes from Munc18c-null mice show increased sensitivity to insulin-stimulated GLUT4 externalization
    • Kanda H., Tamori Y., Shinoda H., Yoshikawa M., Sakaue M., Udagawa J., et al. Adipocytes from Munc18c-null mice show increased sensitivity to insulin-stimulated GLUT4 externalization. J. Clin. Invest. 2005, 115(2):291-301.
    • (2005) J. Clin. Invest. , vol.115 , Issue.2 , pp. 291-301
    • Kanda, H.1    Tamori, Y.2    Shinoda, H.3    Yoshikawa, M.4    Sakaue, M.5    Udagawa, J.6
  • 277
    • 0043268827 scopus 로고    scopus 로고
    • Insulin resistance in tetracycline-repressible Munc18c transgenic mice
    • Spurlin B.A., Thomas R.M., Nevins A.K., Kim H.J., Kim Y.J., Noh H.L., et al. Insulin resistance in tetracycline-repressible Munc18c transgenic mice. Diabetes 2003, 52:1910-1917.
    • (2003) Diabetes , vol.52 , pp. 1910-1917
    • Spurlin, B.A.1    Thomas, R.M.2    Nevins, A.K.3    Kim, H.J.4    Kim, Y.J.5    Noh, H.L.6
  • 278
    • 21744449171 scopus 로고    scopus 로고
    • Identification of 80K-H as a protein involved in GLUT4 vesicle trafficking
    • Hodgkinson C.P., Mander A., Sale G.J. Identification of 80K-H as a protein involved in GLUT4 vesicle trafficking. Biochem. J. 2005, 388(3):785-793.
    • (2005) Biochem. J. , vol.388 , Issue.3 , pp. 785-793
    • Hodgkinson, C.P.1    Mander, A.2    Sale, G.J.3
  • 279
    • 0042818205 scopus 로고    scopus 로고
    • Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation
    • Widberg C.H., Bryant N.J., Girotti M., Rea S., James D.E. Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation. J. Biol. Chem. 2003, 278:35093-35101.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35093-35101
    • Widberg, C.H.1    Bryant, N.J.2    Girotti, M.3    Rea, S.4    James, D.E.5
  • 280
    • 0035121380 scopus 로고    scopus 로고
    • The synaptic vesicle protein, cysteine-string protein, is associated with the plasma membrane in 3T3-L1 adipocytes and interacts with syntaxin 4
    • Chamberlain L.H., Graham M.E., Kane S., Jackson J.L., Maier V.H., Burgoyne R.D., et al. The synaptic vesicle protein, cysteine-string protein, is associated with the plasma membrane in 3T3-L1 adipocytes and interacts with syntaxin 4. J. Cell Sci. 2001, 114:445-455.
    • (2001) J. Cell Sci. , vol.114 , pp. 445-455
    • Chamberlain, L.H.1    Graham, M.E.2    Kane, S.3    Jackson, J.L.4    Maier, V.H.5    Burgoyne, R.D.6
  • 281
    • 0037008753 scopus 로고    scopus 로고
    • Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly
    • Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H. Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly. J. Biol. Chem. 2002, 277:28271-28279.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28271-28279
    • Scales, S.J.1    Hesser, B.A.2    Masuda, E.S.3    Scheller, R.H.4
  • 282
    • 63249132304 scopus 로고    scopus 로고
    • DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes
    • Fukuda N., Emoto M., Nakamori Y., Taguchi A., Miyamoto S., Uraki S., et al. DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes. Diabetes 2009, 58(2):377-384.
    • (2009) Diabetes , vol.58 , Issue.2 , pp. 377-384
    • Fukuda, N.1    Emoto, M.2    Nakamori, Y.3    Taguchi, A.4    Miyamoto, S.5    Uraki, S.6
  • 283
    • 52049101363 scopus 로고    scopus 로고
    • The tyrosine phosphorylation of Munc18c induces a switch in binding specificity from syntaxin 4 to Doc2beta
    • Jewell J.L., Oh E., Bennett S.M., Meroueh S.O., Thurmond D.C. The tyrosine phosphorylation of Munc18c induces a switch in binding specificity from syntaxin 4 to Doc2beta. J. Biol. Chem. 2008, 283(31):21734-21746.
    • (2008) J. Biol. Chem. , vol.283 , Issue.31 , pp. 21734-21746
    • Jewell, J.L.1    Oh, E.2    Bennett, S.M.3    Meroueh, S.O.4    Thurmond, D.C.5
  • 284
    • 38049136729 scopus 로고    scopus 로고
    • Snapin interacts with the Exo70 subunit of the exocyst and modulates GLUT4 trafficking
    • Bao Y., Lopez J.A., James D.E., Hunziker W. Snapin interacts with the Exo70 subunit of the exocyst and modulates GLUT4 trafficking. J. Biol. Chem. 2008, 283(1):324-331.
    • (2008) J. Biol. Chem. , vol.283 , Issue.1 , pp. 324-331
    • Bao, Y.1    Lopez, J.A.2    James, D.E.3    Hunziker, W.4
  • 285
    • 0034695624 scopus 로고    scopus 로고
    • Pantophysin is a phosphoprotein component of adipocyte transport vesicles and associates with GLUT4-containing vesicles
    • Brooks C.C., Scherer P.E., Cleveland K., Whittemore J.L., Lodish H.F., Cheatham B. Pantophysin is a phosphoprotein component of adipocyte transport vesicles and associates with GLUT4-containing vesicles. J. Biol. Chem. 2000, 275:2029-2036.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2029-2036
    • Brooks, C.C.1    Scherer, P.E.2    Cleveland, K.3    Whittemore, J.L.4    Lodish, H.F.5    Cheatham, B.6
  • 286
    • 0034209034 scopus 로고    scopus 로고
    • A functional role for VAP-33 in insulin-stimulated GLUT4 traffic
    • Foster L.J., Weir M.L., Lim D.Y., Liu Z., Trimble W.S., Klip A. A functional role for VAP-33 in insulin-stimulated GLUT4 traffic. Traffic 2000, 1:512-521.
    • (2000) Traffic , vol.1 , pp. 512-521
    • Foster, L.J.1    Weir, M.L.2    Lim, D.Y.3    Liu, Z.4    Trimble, W.S.5    Klip, A.6
  • 287
    • 0033979604 scopus 로고    scopus 로고
    • The transferrin receptor defines two distinct contraction-responsive GLUT4 vesicle populations in skeletal muscle
    • Lemieux K., Han X.X., Dombrowski L., Bonen A., Marette A. The transferrin receptor defines two distinct contraction-responsive GLUT4 vesicle populations in skeletal muscle. Diabetes 2000, 49:183-189.
    • (2000) Diabetes , vol.49 , pp. 183-189
    • Lemieux, K.1    Han, X.X.2    Dombrowski, L.3    Bonen, A.4    Marette, A.5
  • 288
    • 0029064123 scopus 로고
    • Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin
    • Lund S., Holman G.D., Schmitz O., Pedersen O. Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:5817-5821.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5817-5821
    • Lund, S.1    Holman, G.D.2    Schmitz, O.3    Pedersen, O.4
  • 289
    • 33644874487 scopus 로고    scopus 로고
    • Are tyrosine kinases involved in mediating contraction-stimulated muscle glucose transport?
    • Wright D.C., Geiger P.C., Han D.H., Holloszy J.O. Are tyrosine kinases involved in mediating contraction-stimulated muscle glucose transport?. Am. J. Physiol. Endocrinol. Metab. 2006, 290(1):E123-E128.
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.290 , Issue.1
    • Wright, D.C.1    Geiger, P.C.2    Han, D.H.3    Holloszy, J.O.4
  • 290
    • 18344412992 scopus 로고    scopus 로고
    • Evidence against protein kinase B as a mediator of contraction-induced glucose transport and GLUT4 translocation in rat skeletal muscle
    • Lund S., Pryor P.R., Ostergaard S., Schmitz O., Pedersen O., Holman G.D. Evidence against protein kinase B as a mediator of contraction-induced glucose transport and GLUT4 translocation in rat skeletal muscle. FEBS Lett. 1998, 425:472-474.
    • (1998) FEBS Lett. , vol.425 , pp. 472-474
    • Lund, S.1    Pryor, P.R.2    Ostergaard, S.3    Schmitz, O.4    Pedersen, O.5    Holman, G.D.6
  • 291
    • 0842288475 scopus 로고    scopus 로고
    • 2+ and AMPK both mediate stimulation of glucose transport by muscle contractions
    • 2+ and AMPK both mediate stimulation of glucose transport by muscle contractions. Diabetes 2004, 53(2):330-335.
    • (2004) Diabetes , vol.53 , Issue.2 , pp. 330-335
    • Wright, D.C.1    Hucker, K.A.2    Holloszy, J.O.3    Han, D.H.4
  • 292
    • 0242600806 scopus 로고    scopus 로고
    • 5-Amino-imidazole carboxamide riboside increases glucose transport and cell-surface GLUT4 content in skeletal muscle from subjects with type 2 diabetes
    • Koistinen H.A., Galuska D., Chibalin A.V., Yang J., Zierath J.R., Holman G.D., et al. 5-Amino-imidazole carboxamide riboside increases glucose transport and cell-surface GLUT4 content in skeletal muscle from subjects with type 2 diabetes. Diabetes 2003, 52:1066-1072.
    • (2003) Diabetes , vol.52 , pp. 1066-1072
    • Koistinen, H.A.1    Galuska, D.2    Chibalin, A.V.3    Yang, J.4    Zierath, J.R.5    Holman, G.D.6
  • 293
    • 0036165489 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide ribonucleoside treatment improves glucose homeostasis in insulin-resistant diabetic (ob/ob) mice
    • Song X.M., Fiedler M., Galuska D., Ryder J.W., Fernstrom M., Chibalin A.V., et al. 5-Aminoimidazole-4-carboxamide ribonucleoside treatment improves glucose homeostasis in insulin-resistant diabetic (ob/ob) mice. Diabetologia 2002, 45(1):56-65.
    • (2002) Diabetologia , vol.45 , Issue.1 , pp. 56-65
    • Song, X.M.1    Fiedler, M.2    Galuska, D.3    Ryder, J.W.4    Fernstrom, M.5    Chibalin, A.V.6
  • 295
    • 38349019479 scopus 로고    scopus 로고
    • Identification of protein kinase D as a novel contraction-activated kinase linked to GLUT4-mediated glucose uptake, independent of AMPK
    • Luiken J.J., Vertommen D., Coort S.L., Habets D.D., El Hasnaoui M., Pelsers M.M., et al. Identification of protein kinase D as a novel contraction-activated kinase linked to GLUT4-mediated glucose uptake, independent of AMPK. Cell. Signal. 2008, 20(3):543-556.
    • (2008) Cell. Signal. , vol.20 , Issue.3 , pp. 543-556
    • Luiken, J.J.1    Vertommen, D.2    Coort, S.L.3    Habets, D.D.4    El Hasnaoui, M.5    Pelsers, M.M.6
  • 296
    • 84868257195 scopus 로고    scopus 로고
    • Overexpression of vesicle-associated membrane protein (VAMP) 3, but not VAMP2, protects glucose transporter (GLUT) 4 protein translocation in an in vitro model of cardiac insulin resistance
    • Schwenk R.W., Angin Y., Steinbusch L.K., Dirkx E., Hoebers N., Coumans W.A., et al. Overexpression of vesicle-associated membrane protein (VAMP) 3, but not VAMP2, protects glucose transporter (GLUT) 4 protein translocation in an in vitro model of cardiac insulin resistance. J. Biol. Chem. 2012, 287(44):37530-37539.
    • (2012) J. Biol. Chem. , vol.287 , Issue.44 , pp. 37530-37539
    • Schwenk, R.W.1    Angin, Y.2    Steinbusch, L.K.3    Dirkx, E.4    Hoebers, N.5    Coumans, W.A.6
  • 297
    • 77958046738 scopus 로고    scopus 로고
    • Requirement for distinct vesicle-associated membrane proteins in insulin- and AMP-activated protein kinase (AMPK)-induced translocation of GLUT4 and CD36 in cultured cardiomyocytes
    • Schwenk R.W., Dirkx E., Coumans W.A., Bonen A., Klip A., Glatz J.F., et al. Requirement for distinct vesicle-associated membrane proteins in insulin- and AMP-activated protein kinase (AMPK)-induced translocation of GLUT4 and CD36 in cultured cardiomyocytes. Diabetologia 2010, 53(10):2209-2219.
    • (2010) Diabetologia , vol.53 , Issue.10 , pp. 2209-2219
    • Schwenk, R.W.1    Dirkx, E.2    Coumans, W.A.3    Bonen, A.4    Klip, A.5    Glatz, J.F.6
  • 298
    • 84884742734 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate 5-kinase (PIKfyve) is an AMPK target participating in contraction-stimulated glucose uptake in skeletal muscle
    • Liu Y., Lai Y.C., Hill E.V., Tyteca D., Carpentier S., Ingvaldsen A., et al. Phosphatidylinositol 3-phosphate 5-kinase (PIKfyve) is an AMPK target participating in contraction-stimulated glucose uptake in skeletal muscle. Biochem. J. 2013, 455(2):195-206.
    • (2013) Biochem. J. , vol.455 , Issue.2 , pp. 195-206
    • Liu, Y.1    Lai, Y.C.2    Hill, E.V.3    Tyteca, D.4    Carpentier, S.5    Ingvaldsen, A.6
  • 299
    • 36849069450 scopus 로고    scopus 로고
    • Calmodulin-binding domain of AS160 regulates contraction- but not insulin-stimulated glucose uptake in skeletal muscle
    • Kramer H.F., Taylor E.B., Witczak C.A., Fujii N., Hirshman M.F., Goodyear L.J. Calmodulin-binding domain of AS160 regulates contraction- but not insulin-stimulated glucose uptake in skeletal muscle. Diabetes 2007, 56(12):2854-2862.
    • (2007) Diabetes , vol.56 , Issue.12 , pp. 2854-2862
    • Kramer, H.F.1    Taylor, E.B.2    Witczak, C.A.3    Fujii, N.4    Hirshman, M.F.5    Goodyear, L.J.6
  • 300
    • 33845998942 scopus 로고    scopus 로고
    • AS160 regulates insulin- and contraction-stimulated glucose uptake in mouse skeletal muscle
    • Kramer H.F., Witczak C.A., Taylor E.B., Fujii N., Hirshman M.F., Goodyear L.J. AS160 regulates insulin- and contraction-stimulated glucose uptake in mouse skeletal muscle. J. Biol. Chem. 2006, 281(42):31478-31485.
    • (2006) J. Biol. Chem. , vol.281 , Issue.42 , pp. 31478-31485
    • Kramer, H.F.1    Witczak, C.A.2    Taylor, E.B.3    Fujii, N.4    Hirshman, M.F.5    Goodyear, L.J.6
  • 301
    • 33747039008 scopus 로고    scopus 로고
    • Distinct signals regulate AS160 phosphorylation in response to insulin, AICAR, and contraction in mouse skeletal muscle
    • Kramer H.F., Witczak C.A., Fujii N., Jessen N., Taylor E.B., Arnolds D.E., et al. Distinct signals regulate AS160 phosphorylation in response to insulin, AICAR, and contraction in mouse skeletal muscle. Diabetes 2006, 55(7):2067-2076.
    • (2006) Diabetes , vol.55 , Issue.7 , pp. 2067-2076
    • Kramer, H.F.1    Witczak, C.A.2    Fujii, N.3    Jessen, N.4    Taylor, E.B.5    Arnolds, D.E.6
  • 302
    • 44049087531 scopus 로고    scopus 로고
    • Inhibition of GLUT4 translocation by Tbc1d1, a Rab GTPase-activating protein abundant in skeletal muscle, is partially relieved by AMP-activated protein kinase activation
    • Chavez J.A., Roach W.G., Keller S.R., Lane W.S., Lienhard G.E. Inhibition of GLUT4 translocation by Tbc1d1, a Rab GTPase-activating protein abundant in skeletal muscle, is partially relieved by AMP-activated protein kinase activation. J. Biol. Chem. 2008, 283(14):9187-9195.
    • (2008) J. Biol. Chem. , vol.283 , Issue.14 , pp. 9187-9195
    • Chavez, J.A.1    Roach, W.G.2    Keller, S.R.3    Lane, W.S.4    Lienhard, G.E.5
  • 303
    • 71049147903 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of the Rab GTPase-activating protein TBC1D1 regulates GLUT4 translocation
    • Peck G.R., Chavez J.A., Roach W.G., Budnik B.A., Lane W.S., Karlsson H.K., et al. Insulin-stimulated phosphorylation of the Rab GTPase-activating protein TBC1D1 regulates GLUT4 translocation. J. Biol. Chem. 2009, 284(44):30016-30023.
    • (2009) J. Biol. Chem. , vol.284 , Issue.44 , pp. 30016-30023
    • Peck, G.R.1    Chavez, J.A.2    Roach, W.G.3    Budnik, B.A.4    Lane, W.S.5    Karlsson, H.K.6
  • 304
    • 44349161745 scopus 로고    scopus 로고
    • Discovery of TBC1D1 as an insulin-, AICAR-, and contraction-stimulated signaling nexus in mouse skeletal muscle
    • Taylor E.B., An D., Kramer H.F., Yu H., Fujii N.L., Roeckl K.S., et al. Discovery of TBC1D1 as an insulin-, AICAR-, and contraction-stimulated signaling nexus in mouse skeletal muscle. J. Biol. Chem. 2008, 283(15):9787-9796.
    • (2008) J. Biol. Chem. , vol.283 , Issue.15 , pp. 9787-9796
    • Taylor, E.B.1    An, D.2    Kramer, H.F.3    Yu, H.4    Fujii, N.L.5    Roeckl, K.S.6
  • 305
    • 78650549552 scopus 로고    scopus 로고
    • Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation in muscle cells
    • Sun Y., Bilan P.J., Liu Z., Klip A. Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation in muscle cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107(46):19909-19914.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.46 , pp. 19909-19914
    • Sun, Y.1    Bilan, P.J.2    Liu, Z.3    Klip, A.4
  • 306
    • 84876526228 scopus 로고    scopus 로고
    • Electrical stimuli release ATP to increase GLUT4 translocation and glucose uptake via PI3Kgamma-Akt-AS160 in skeletal muscle cells
    • Osorio-Fuentealba C., Contreras-Ferrat A.E., Altamirano F., Espinosa A., Li Q., Niu W., et al. Electrical stimuli release ATP to increase GLUT4 translocation and glucose uptake via PI3Kgamma-Akt-AS160 in skeletal muscle cells. Diabetes 2013, 62(5):1519-1526.
    • (2013) Diabetes , vol.62 , Issue.5 , pp. 1519-1526
    • Osorio-Fuentealba, C.1    Contreras-Ferrat, A.E.2    Altamirano, F.3    Espinosa, A.4    Li, Q.5    Niu, W.6
  • 307
    • 33846178185 scopus 로고    scopus 로고
    • Rabs 8A and 14 are targets of the insulin-regulated Rab-GAP AS160 regulating GLUT4 traffic in muscle cells
    • Ishikura S., Bilan P.J., Klip A. Rabs 8A and 14 are targets of the insulin-regulated Rab-GAP AS160 regulating GLUT4 traffic in muscle cells. Biochem. Biophys. Res. Commun. 2007, 353(4):1074-1079.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , Issue.4 , pp. 1074-1079
    • Ishikura, S.1    Bilan, P.J.2    Klip, A.3
  • 308
    • 84898758717 scopus 로고    scopus 로고
    • Myosin Va mediates Rab8A-regulated GLUT4 vesicle exocytosis in insulin-stimulated muscle cells
    • Sun Y., Chiu T.T., Foley K.P., Bilan P.J., Klip A. Myosin Va mediates Rab8A-regulated GLUT4 vesicle exocytosis in insulin-stimulated muscle cells. Mol. Biol. Cell 2014, 25(7):1159-1170.
    • (2014) Mol. Biol. Cell , vol.25 , Issue.7 , pp. 1159-1170
    • Sun, Y.1    Chiu, T.T.2    Foley, K.P.3    Bilan, P.J.4    Klip, A.5
  • 309
    • 0030659755 scopus 로고    scopus 로고
    • GLUT4 vesicle dynamics in living 3T3L1 adipocytes visualized with green-fluorescent protein
    • Oatey P.B., Van Weering D.H., Dobson S.P., Gould G.W., Tavare J.M. GLUT4 vesicle dynamics in living 3T3L1 adipocytes visualized with green-fluorescent protein. Biochem. J. 1997, 327:637-642.
    • (1997) Biochem. J. , vol.327 , pp. 637-642
    • Oatey, P.B.1    Van Weering, D.H.2    Dobson, S.P.3    Gould, G.W.4    Tavare, J.M.5
  • 310
    • 33845973390 scopus 로고    scopus 로고
    • Microtubule network is required for insulin signaling through activation of Akt/protein kinase B: evidence that insulin stimulates vesicle docking/fusion but not intracellular mobility
    • Eyster C.A., Duggins Q.S., Gorbsky G.J., Olson A.L. Microtubule network is required for insulin signaling through activation of Akt/protein kinase B: evidence that insulin stimulates vesicle docking/fusion but not intracellular mobility. J. Biol. Chem. 2006, 281(51):39719-39727.
    • (2006) J. Biol. Chem. , vol.281 , Issue.51 , pp. 39719-39727
    • Eyster, C.A.1    Duggins, Q.S.2    Gorbsky, G.J.3    Olson, A.L.4
  • 311
    • 0038242297 scopus 로고    scopus 로고
    • Conventional kinesin KIF5B mediates insulin-stimulated GLUT4 movements on microtubules
    • Semiz S., Park J.G., Nicoloro S.M., Furcinitti P., Zhang C., Chawla A., et al. Conventional kinesin KIF5B mediates insulin-stimulated GLUT4 movements on microtubules. EMBO J. 2003, 22:2387-2399.
    • (2003) EMBO J. , vol.22 , pp. 2387-2399
    • Semiz, S.1    Park, J.G.2    Nicoloro, S.M.3    Furcinitti, P.4    Zhang, C.5    Chawla, A.6
  • 312
    • 44549084822 scopus 로고    scopus 로고
    • Selective regulation of the perinuclear distribution of glucose transporter 4 (GLUT4) by insulin signals in muscle cells
    • Dugani C.B., Randhawa V.K., Cheng A.W., Patel N., Klip A. Selective regulation of the perinuclear distribution of glucose transporter 4 (GLUT4) by insulin signals in muscle cells. Eur. J. Cell Biol. 2008, 87(6):337-351.
    • (2008) Eur. J. Cell Biol. , vol.87 , Issue.6 , pp. 337-351
    • Dugani, C.B.1    Randhawa, V.K.2    Cheng, A.W.3    Patel, N.4    Klip, A.5
  • 313
    • 73949110560 scopus 로고    scopus 로고
    • The t-SNAREs syntaxin4 and SNAP23 but not v-SNARE VAMP2 are indispensable to tether GLUT4 vesicles at the plasma membrane in adipocyte
    • Kawaguchi T., Tamori Y., Kanda H., Yoshikawa M., Tateya S., Nishino N., et al. The t-SNAREs syntaxin4 and SNAP23 but not v-SNARE VAMP2 are indispensable to tether GLUT4 vesicles at the plasma membrane in adipocyte. Biochem. Biophys. Res. Commun. 2010, 391(3):1336-1341.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , Issue.3 , pp. 1336-1341
    • Kawaguchi, T.1    Tamori, Y.2    Kanda, H.3    Yoshikawa, M.4    Tateya, S.5    Nishino, N.6
  • 314
    • 0035176823 scopus 로고    scopus 로고
    • Insulin action on GLUT4 traffic visualized in single 3T3-l1 adipocytes by using ultra-fast microscopy
    • Patki V., Buxton J., Chawla A., Lifshitz L., Fogarty K., Carrington W., et al. Insulin action on GLUT4 traffic visualized in single 3T3-l1 adipocytes by using ultra-fast microscopy. Mol. Biol. Cell 2001, 12:129-141.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 129-141
    • Patki, V.1    Buxton, J.2    Chawla, A.3    Lifshitz, L.4    Fogarty, K.5    Carrington, W.6
  • 315
    • 33947606334 scopus 로고    scopus 로고
    • Insulin stimulates membrane fusion and GLUT4 accumulation in clathrin coats on adipocyte plasma membranes
    • Huang S., Lifshitz L.M., Jones C., Bellve K.D., Standley C., Fonseca S., et al. Insulin stimulates membrane fusion and GLUT4 accumulation in clathrin coats on adipocyte plasma membranes. Mol. Cell Biol. 2007, 27(9):3456-3469.
    • (2007) Mol. Cell Biol. , vol.27 , Issue.9 , pp. 3456-3469
    • Huang, S.1    Lifshitz, L.M.2    Jones, C.3    Bellve, K.D.4    Standley, C.5    Fonseca, S.6
  • 316
    • 84887363321 scopus 로고    scopus 로고
    • Impaired tethering and fusion of GLUT4 vesicles in insulin-resistant human adipose cells
    • Lizunov V.A., Lee J.P., Skarulis M.C., Zimmerberg J., Cushman S.W., Stenkula K.G. Impaired tethering and fusion of GLUT4 vesicles in insulin-resistant human adipose cells. Diabetes 2013, 62(9):3114-3119.
    • (2013) Diabetes , vol.62 , Issue.9 , pp. 3114-3119
    • Lizunov, V.A.1    Lee, J.P.2    Skarulis, M.C.3    Zimmerberg, J.4    Cushman, S.W.5    Stenkula, K.G.6
  • 317
    • 19644377176 scopus 로고    scopus 로고
    • Insulin-stimulated plasma membrane fusion of GLUT4 glucose transporter-containing vesicles is regulated by phospholipase D1
    • Huang P., Altshuller Y.M., Hou J.C., Pessin J.E., Frohman M.A. Insulin-stimulated plasma membrane fusion of GLUT4 glucose transporter-containing vesicles is regulated by phospholipase D1. Mol. Biol. Cell 2005, 16(6):2614-2623.
    • (2005) Mol. Biol. Cell , vol.16 , Issue.6 , pp. 2614-2623
    • Huang, P.1    Altshuller, Y.M.2    Hou, J.C.3    Pessin, J.E.4    Frohman, M.A.5
  • 320
    • 4744362873 scopus 로고    scopus 로고
    • Insulin stimulates the entry of GLUT4 into the endosomal recycling pathway by a quantal mechanism
    • Coster A.C., Govers R., James D.E. Insulin stimulates the entry of GLUT4 into the endosomal recycling pathway by a quantal mechanism. Traffic 2004, 5:763-771.
    • (2004) Traffic , vol.5 , pp. 763-771
    • Coster, A.C.1    Govers, R.2    James, D.E.3
  • 321
    • 0025761381 scopus 로고
    • Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat
    • Slot J.W., Geuze H.J., Gigengack S., Lienhard G.E., James D.E. Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat. J. Cell Biol. 1991, 113:123-135.
    • (1991) J. Cell Biol. , vol.113 , pp. 123-135
    • Slot, J.W.1    Geuze, H.J.2    Gigengack, S.3    Lienhard, G.E.4    James, D.E.5
  • 322
    • 0035941297 scopus 로고    scopus 로고
    • Insulin accelerates inter-endosomal GLUT4 traffic via phosphatidylinositol 3-kinase and protein kinase B
    • Foster L.J., Li D., Randhawa V.K., Klip A. Insulin accelerates inter-endosomal GLUT4 traffic via phosphatidylinositol 3-kinase and protein kinase B. J. Biol. Chem. 2001, 276:44212-44221.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44212-44221
    • Foster, L.J.1    Li, D.2    Randhawa, V.K.3    Klip, A.4
  • 323
    • 74449092996 scopus 로고    scopus 로고
    • GLUT4 molecules are recruited at random for insertion within the plasma membrane upon insulin stimulation
    • Berenguer M., Le Marchand-Brustel Y., Govers R. GLUT4 molecules are recruited at random for insertion within the plasma membrane upon insulin stimulation. FEBS Lett. 2010, 584(3):537-542.
    • (2010) FEBS Lett. , vol.584 , Issue.3 , pp. 537-542
    • Berenguer, M.1    Le Marchand-Brustel, Y.2    Govers, R.3
  • 324
    • 0029966086 scopus 로고    scopus 로고
    • Insulin-mediated targeting of phosphatidylinositol 3-kinase to GLUT4-containing vesicles
    • Heller-Harrison R.A., Morin M., Guilherme A., Czech M.P. Insulin-mediated targeting of phosphatidylinositol 3-kinase to GLUT4-containing vesicles. J. Biol. Chem. 1996, 271:10200-10204.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10200-10204
    • Heller-Harrison, R.A.1    Morin, M.2    Guilherme, A.3    Czech, M.P.4
  • 326
    • 84891679672 scopus 로고    scopus 로고
    • Prolonged insulin stimulation down-regulates GLUT4 through oxidative stress-mediated retromer inhibition by a protein kinase CK2-dependent mechanism in 3T3-L1 adipocytes
    • Ma J., Nakagawa Y., Kojima I., Shibata H. Prolonged insulin stimulation down-regulates GLUT4 through oxidative stress-mediated retromer inhibition by a protein kinase CK2-dependent mechanism in 3T3-L1 adipocytes. J. Biol. Chem. 2014, 289(1):133-142.
    • (2014) J. Biol. Chem. , vol.289 , Issue.1 , pp. 133-142
    • Ma, J.1    Nakagawa, Y.2    Kojima, I.3    Shibata, H.4
  • 327
    • 0027290847 scopus 로고
    • Use of bismannose photolabel to elucidate insulin-regulated GLUT4 subcellular trafficking kinetics in rat adipose cells. Evidence that exocytosis is a critical site of hormone action
    • Satoh S., Nishimura H., Clark A.E., Kozka I.J., Vannucci S.J., Simpson I.A., et al. Use of bismannose photolabel to elucidate insulin-regulated GLUT4 subcellular trafficking kinetics in rat adipose cells. Evidence that exocytosis is a critical site of hormone action. J. Biol. Chem. 1993, 268:17820-17829.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17820-17829
    • Satoh, S.1    Nishimura, H.2    Clark, A.E.3    Kozka, I.J.4    Vannucci, S.J.5    Simpson, I.A.6
  • 328
    • 0027532611 scopus 로고
    • Comparison of GLUT4 and GLUT1 subcellular trafficking in basal and insulin-stimulated 3T3-L1 cells
    • Yang J., Holman G.D. Comparison of GLUT4 and GLUT1 subcellular trafficking in basal and insulin-stimulated 3T3-L1 cells. J. Biol. Chem. 1993, 268:4600-4603.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4600-4603
    • Yang, J.1    Holman, G.D.2
  • 329
    • 0034622517 scopus 로고    scopus 로고
    • Modulation of GLUT4 and GLUT1 recycling by insulin in rat adipocytes: kinetic analysis based on the involvement of multiple intracellular compartments
    • Lee W., Ryu J., Spangler R.A., Jung C.Y. Modulation of GLUT4 and GLUT1 recycling by insulin in rat adipocytes: kinetic analysis based on the involvement of multiple intracellular compartments. Biochemistry 2000, 39:9358-9366.
    • (2000) Biochemistry , vol.39 , pp. 9358-9366
    • Lee, W.1    Ryu, J.2    Spangler, R.A.3    Jung, C.Y.4
  • 330
    • 33845688698 scopus 로고    scopus 로고
    • GLUT4 is internalized by a cholesterol-dependent nystatin-sensitive mechanism inhibited by insulin
    • Blot V., McGraw T.E. GLUT4 is internalized by a cholesterol-dependent nystatin-sensitive mechanism inhibited by insulin. EMBO J. 2006, 25(24):5648-5658.
    • (2006) EMBO J. , vol.25 , Issue.24 , pp. 5648-5658
    • Blot, V.1    McGraw, T.E.2
  • 331
    • 77956298609 scopus 로고    scopus 로고
    • Insulin controls the spatial distribution of GLUT4 on the cell surface through regulation of its postfusion dispersal
    • Stenkula K.G., Lizunov V.A., Cushman S.W., Zimmerberg J. Insulin controls the spatial distribution of GLUT4 on the cell surface through regulation of its postfusion dispersal. Cell Metab. 2010, 12(3):250-259.
    • (2010) Cell Metab. , vol.12 , Issue.3 , pp. 250-259
    • Stenkula, K.G.1    Lizunov, V.A.2    Cushman, S.W.3    Zimmerberg, J.4
  • 333
    • 0024314795 scopus 로고
    • Plasma membrane lipid order and composition during adipocyte differentiation of 3T3F442A cells. Studies in intact cells with 1-[4-(trimethylamino)phenyl]-6-phenylhexatriene
    • Storch J., Shulman S.L., Kleinfeld A.M. Plasma membrane lipid order and composition during adipocyte differentiation of 3T3F442A cells. Studies in intact cells with 1-[4-(trimethylamino)phenyl]-6-phenylhexatriene. J. Biol. Chem. 1989, 264(18):10527-10533.
    • (1989) J. Biol. Chem. , vol.264 , Issue.18 , pp. 10527-10533
    • Storch, J.1    Shulman, S.L.2    Kleinfeld, A.M.3
  • 334
    • 79952452973 scopus 로고    scopus 로고
    • Dimethyl sulfoxide enhances GLUT4 translocation through a reduction in GLUT4 endocytosis in insulin-stimulated 3T3-L1 adipocytes
    • Berenguer M., Zhang J., Bruce M.C., Martinez L., Gonzalez T., Gurtovenko A.A., et al. Dimethyl sulfoxide enhances GLUT4 translocation through a reduction in GLUT4 endocytosis in insulin-stimulated 3T3-L1 adipocytes. Biochimie 2011, 93(4):697-709.
    • (2011) Biochimie , vol.93 , Issue.4 , pp. 697-709
    • Berenguer, M.1    Zhang, J.2    Bruce, M.C.3    Martinez, L.4    Gonzalez, T.5    Gurtovenko, A.A.6
  • 335
    • 0034907579 scopus 로고    scopus 로고
    • Insulin-induced cortical actin remodeling promotes GLUT4 insertion at muscle cell membrane ruffles
    • Tong P., Khayat Z.A., Huang C., Patel N., Ueyama A., Klip A. Insulin-induced cortical actin remodeling promotes GLUT4 insertion at muscle cell membrane ruffles. J. Clin. Invest. 2001, 108:371-381.
    • (2001) J. Clin. Invest. , vol.108 , pp. 371-381
    • Tong, P.1    Khayat, Z.A.2    Huang, C.3    Patel, N.4    Ueyama, A.5    Klip, A.6
  • 336
    • 0035834644 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling
    • Kanzaki M., Pessin J.E. Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling. J. Biol. Chem. 2001, 276:42436-42444.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42436-42444
    • Kanzaki, M.1    Pessin, J.E.2
  • 337
    • 70349307380 scopus 로고    scopus 로고
    • Identification of a distal GLUT4 trafficking event controlled by actin polymerization
    • Lopez J.A., Burchfield J.G., Blair D.H., Mele K., Ng Y., Vallotton P., et al. Identification of a distal GLUT4 trafficking event controlled by actin polymerization. Mol. Biol. Cell 2009, 20(17):3918-3929.
    • (2009) Mol. Biol. Cell , vol.20 , Issue.17 , pp. 3918-3929
    • Lopez, J.A.1    Burchfield, J.G.2    Blair, D.H.3    Mele, K.4    Ng, Y.5    Vallotton, P.6
  • 338
    • 0033962410 scopus 로고    scopus 로고
    • Insulin-induced actin filament remodeling colocalizes actin with phosphatidylinositol 3-kinase and GLUT4 in L6 myotubes
    • Khayat Z.A., Tong P., Yaworsky K., Bloch R.J., Klip A. Insulin-induced actin filament remodeling colocalizes actin with phosphatidylinositol 3-kinase and GLUT4 in L6 myotubes. J. Cell Sci. 2000, 113(2):279-290.
    • (2000) J. Cell Sci. , vol.113 , Issue.2 , pp. 279-290
    • Khayat, Z.A.1    Tong, P.2    Yaworsky, K.3    Bloch, R.J.4    Klip, A.5
  • 339
    • 56149122236 scopus 로고    scopus 로고
    • Activation of the small GTPase Rac1 by a specific guanine-nucleotide-exchange factor suffices to induce glucose uptake into skeletal-muscle cells
    • Ueda S., Kataoka T., Satoh T. Activation of the small GTPase Rac1 by a specific guanine-nucleotide-exchange factor suffices to induce glucose uptake into skeletal-muscle cells. Biol. Cell 2008, 100(11):645-657.
    • (2008) Biol. Cell , vol.100 , Issue.11 , pp. 645-657
    • Ueda, S.1    Kataoka, T.2    Satoh, T.3
  • 340
    • 77954447111 scopus 로고    scopus 로고
    • Crucial role of the small GTPase Rac1 in insulin-stimulated translocation of glucose transporter 4 to the mouse skeletal muscle sarcolemma
    • Ueda S., Kitazawa S., Ishida K., Nishikawa Y., Matsui M., Matsumoto H., et al. Crucial role of the small GTPase Rac1 in insulin-stimulated translocation of glucose transporter 4 to the mouse skeletal muscle sarcolemma. FASEB J. 2010, 24(7):2254-2261.
    • (2010) FASEB J. , vol.24 , Issue.7 , pp. 2254-2261
    • Ueda, S.1    Kitazawa, S.2    Ishida, K.3    Nishikawa, Y.4    Matsui, M.5    Matsumoto, H.6
  • 341
    • 83355166914 scopus 로고    scopus 로고
    • Identification of P-Rex1 as a novel Rac1-guanine nucleotide exchange factor (GEF) that promotes actin remodeling and GLUT4 protein trafficking in adipocytes
    • Balamatsias D., Kong A.M., Waters J.E., Sriratana A., Gurung R., Bailey C.G., et al. Identification of P-Rex1 as a novel Rac1-guanine nucleotide exchange factor (GEF) that promotes actin remodeling and GLUT4 protein trafficking in adipocytes. J. Biol. Chem. 2011, 286(50):43229-43240.
    • (2011) J. Biol. Chem. , vol.286 , Issue.50 , pp. 43229-43240
    • Balamatsias, D.1    Kong, A.M.2    Waters, J.E.3    Sriratana, A.4    Gurung, R.5    Bailey, C.G.6
  • 342
    • 84876334507 scopus 로고    scopus 로고
    • Akt2 regulates Rac1 activity in the insulin-dependent signaling pathway leading to GLUT4 translocation to the plasma membrane in skeletal muscle cells
    • Nozaki S., Takeda T., Kitaura T., Takenaka N., Kataoka T., Satoh T. Akt2 regulates Rac1 activity in the insulin-dependent signaling pathway leading to GLUT4 translocation to the plasma membrane in skeletal muscle cells. Cell. Signal. 2013, 25(6):1361-1371.
    • (2013) Cell. Signal. , vol.25 , Issue.6 , pp. 1361-1371
    • Nozaki, S.1    Takeda, T.2    Kitaura, T.3    Takenaka, N.4    Kataoka, T.5    Satoh, T.6
  • 343
    • 84895461940 scopus 로고    scopus 로고
    • A critical role of the small GTPase Rac1 in Akt2-mediated GLUT4 translocation in mouse skeletal muscle
    • Takenaka N., Izawa R., Wu J., Kitagawa K., Nihata Y., Hosooka T., et al. A critical role of the small GTPase Rac1 in Akt2-mediated GLUT4 translocation in mouse skeletal muscle. FEBS J. 2014, 281(5):1493-1504.
    • (2014) FEBS J. , vol.281 , Issue.5 , pp. 1493-1504
    • Takenaka, N.1    Izawa, R.2    Wu, J.3    Kitagawa, K.4    Nihata, Y.5    Hosooka, T.6
  • 344
    • 84890036070 scopus 로고    scopus 로고
    • Akt and Rac1 signaling are jointly required for insulin-stimulated glucose uptake in skeletal muscle and downregulated in insulin resistance
    • Sylow L., Kleinert M., Pehmoller C., Prats C., Chiu T.T., Klip A., et al. Akt and Rac1 signaling are jointly required for insulin-stimulated glucose uptake in skeletal muscle and downregulated in insulin resistance. Cell. Signal. 2014, 26(2):323-331.
    • (2014) Cell. Signal. , vol.26 , Issue.2 , pp. 323-331
    • Sylow, L.1    Kleinert, M.2    Pehmoller, C.3    Prats, C.4    Chiu, T.T.5    Klip, A.6
  • 345
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radhakrishna H., Al-Awar O., Khachikian Z., Donaldson J.G. ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell Sci. 1999, 112:855-866.
    • (1999) J. Cell Sci. , vol.112 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 346
    • 84878242738 scopus 로고    scopus 로고
    • Rac1 signaling is required for insulin-stimulated glucose uptake and is dysregulated in insulin-resistant murine and human skeletal muscle
    • Sylow L., Jensen T.E., Kleinert M., Hojlund K., Kiens B., Wojtaszewski J., et al. Rac1 signaling is required for insulin-stimulated glucose uptake and is dysregulated in insulin-resistant murine and human skeletal muscle. Diabetes 2013, 62(6):1865-1875.
    • (2013) Diabetes , vol.62 , Issue.6 , pp. 1865-1875
    • Sylow, L.1    Jensen, T.E.2    Kleinert, M.3    Hojlund, K.4    Kiens, B.5    Wojtaszewski, J.6
  • 347
    • 0038190982 scopus 로고    scopus 로고
    • Cdc42 is a Rho GTPase family member that can mediate insulin signaling to glucose transport in 3T3-L1 adipocytes
    • Usui I., Imamura T., Huang J., Satoh H., Olefsky J.M. Cdc42 is a Rho GTPase family member that can mediate insulin signaling to glucose transport in 3T3-L1 adipocytes. J. Biol. Chem. 2003, 278:13765-13774.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13765-13774
    • Usui, I.1    Imamura, T.2    Huang, J.3    Satoh, H.4    Olefsky, J.M.5
  • 348
    • 1642546558 scopus 로고    scopus 로고
    • Annexin II is a thiazolidinedione-responsive gene involved in insulin-induced glucose transporter isoform 4 translocation in 3T3-L1 adipocytes
    • Huang J., Hsia S.H., Imamura T., Usui I., Olefsky J.M. Annexin II is a thiazolidinedione-responsive gene involved in insulin-induced glucose transporter isoform 4 translocation in 3T3-L1 adipocytes. Endocrinology 2004, 145(4):1579-1586.
    • (2004) Endocrinology , vol.145 , Issue.4 , pp. 1579-1586
    • Huang, J.1    Hsia, S.H.2    Imamura, T.3    Usui, I.4    Olefsky, J.M.5
  • 349
    • 54449097591 scopus 로고    scopus 로고
    • Alpha-actinin-4 is selectively required for insulin-induced GLUT4 translocation
    • Talior-Volodarsky I., Randhawa V.K., Zaid H., Klip A. Alpha-actinin-4 is selectively required for insulin-induced GLUT4 translocation. J. Biol. Chem. 2008, 283(37):25115-25123.
    • (2008) J. Biol. Chem. , vol.283 , Issue.37 , pp. 25115-25123
    • Talior-Volodarsky, I.1    Randhawa, V.K.2    Zaid, H.3    Klip, A.4
  • 351
    • 54849439728 scopus 로고    scopus 로고
    • CaMKII-mediated phosphorylation of the myosin motor Myo1c is required for insulin-stimulated GLUT4 translocation in adipocytes
    • Yip M.F., Ramm G., Larance M., Hoehn K.L., Wagner M.C., Guilhaus M., et al. CaMKII-mediated phosphorylation of the myosin motor Myo1c is required for insulin-stimulated GLUT4 translocation in adipocytes. Cell Metab. 2008, 8(5):384-398.
    • (2008) Cell Metab. , vol.8 , Issue.5 , pp. 384-398
    • Yip, M.F.1    Ramm, G.2    Larance, M.3    Hoehn, K.L.4    Wagner, M.C.5    Guilhaus, M.6
  • 352
    • 34548188298 scopus 로고    scopus 로고
    • Activation of RalA is required for insulin-stimulated GLUT4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c
    • Chen X.W., Leto D., Chiang S.H., Wang Q., Saltiel A.R. Activation of RalA is required for insulin-stimulated GLUT4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c. Dev. Cell 2007, 13(3):391-404.
    • (2007) Dev. Cell , vol.13 , Issue.3 , pp. 391-404
    • Chen, X.W.1    Leto, D.2    Chiang, S.H.3    Wang, Q.4    Saltiel, A.R.5
  • 353
    • 84865337975 scopus 로고    scopus 로고
    • Role of RalA downstream of Rac1 in insulin-dependent glucose uptake in muscle cells
    • Nozaki S., Ueda S., Takenaka N., Kataoka T., Satoh T. Role of RalA downstream of Rac1 in insulin-dependent glucose uptake in muscle cells. Cell. Signal. 2012, 24(11):2111-2117.
    • (2012) Cell. Signal. , vol.24 , Issue.11 , pp. 2111-2117
    • Nozaki, S.1    Ueda, S.2    Takenaka, N.3    Kataoka, T.4    Satoh, T.5
  • 354
    • 33646791172 scopus 로고    scopus 로고
    • Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes
    • Choi Y.O., Ryu H.J., Kim H.R., Song Y.S., Kim C., Lee W., et al. Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes. Exp. Mol. Med. 2006, 38(2):180-189.
    • (2006) Exp. Mol. Med. , vol.38 , Issue.2 , pp. 180-189
    • Choi, Y.O.1    Ryu, H.J.2    Kim, H.R.3    Song, Y.S.4    Kim, C.5    Lee, W.6
  • 355
    • 53049092872 scopus 로고    scopus 로고
    • Dual role for myosin II in GLUT4-mediated glucose uptake in 3T3-L1 adipocytes
    • Fulcher F.K., Smith B.T., Russ M., Patel Y.M. Dual role for myosin II in GLUT4-mediated glucose uptake in 3T3-L1 adipocytes. Exp. Cell Res. 2008, 314(17):3264-3274.
    • (2008) Exp. Cell Res. , vol.314 , Issue.17 , pp. 3264-3274
    • Fulcher, F.K.1    Smith, B.T.2    Russ, M.3    Patel, Y.M.4
  • 356
    • 72949104129 scopus 로고    scopus 로고
    • Myosin IIA participates in docking of Glut4 storage vesicles with the plasma membrane in 3T3-L1 adipocytes
    • Chung le T.K., Hosaka T., Harada N., Jambaldorj B., Fukunaga K., Nishiwaki Y., et al. Myosin IIA participates in docking of Glut4 storage vesicles with the plasma membrane in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 2010, 391(1):995-999.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , Issue.1 , pp. 995-999
    • Chung le, T.K.1    Hosaka, T.2    Harada, N.3    Jambaldorj, B.4    Fukunaga, K.5    Nishiwaki, Y.6
  • 357
    • 0031576535 scopus 로고    scopus 로고
    • A myosin-derived peptide C109 binds to GLUT4-vesicles and inhibits the insulin-induced glucose transport stimulation and GLUT4 recruitment in rat adipocytes
    • Lee W., Samuel J., Zhang W., Rampal A.L., Lachaal M., Jung C.Y. A myosin-derived peptide C109 binds to GLUT4-vesicles and inhibits the insulin-induced glucose transport stimulation and GLUT4 recruitment in rat adipocytes. Biochem. Biophys. Res. Commun. 1997, 240:409-414.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 409-414
    • Lee, W.1    Samuel, J.2    Zhang, W.3    Rampal, A.L.4    Lachaal, M.5    Jung, C.Y.6
  • 358
    • 0041528537 scopus 로고    scopus 로고
    • Insulin recruits GLUT4 from distinct compartments via distinct traffic pathways with differential microtubule dependence in rat adipocytes
    • Liu L.B., Omata W., Kojima I., Shibata H. Insulin recruits GLUT4 from distinct compartments via distinct traffic pathways with differential microtubule dependence in rat adipocytes. J. Biol. Chem. 2003, 278:30157-30169.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30157-30169
    • Liu, L.B.1    Omata, W.2    Kojima, I.3    Shibata, H.4
  • 359
    • 29644444041 scopus 로고    scopus 로고
    • Disruption of microtubules ablates the specificity of insulin signaling to GLUT4 translocation in 3T3-L1 adipocytes
    • Huang J., Imamura T., Babendure J.L., Lu J.C., Olefsky J.M. Disruption of microtubules ablates the specificity of insulin signaling to GLUT4 translocation in 3T3-L1 adipocytes. J. Biol. Chem. 2005, 280(51):42300-42306.
    • (2005) J. Biol. Chem. , vol.280 , Issue.51 , pp. 42300-42306
    • Huang, J.1    Imamura, T.2    Babendure, J.L.3    Lu, J.C.4    Olefsky, J.M.5
  • 360
    • 0242552004 scopus 로고    scopus 로고
    • Insulin promotes formation of polymerized microtubules by a phosphatidylinositol 3-kinase-independent, actin-dependent pathway in 3T3-L1 adipocytes
    • Olson A.L., Eyster C.A., Duggins Q.S., Knight J.B. Insulin promotes formation of polymerized microtubules by a phosphatidylinositol 3-kinase-independent, actin-dependent pathway in 3T3-L1 adipocytes. Endocrinology 2003, 144(11):5030-5039.
    • (2003) Endocrinology , vol.144 , Issue.11 , pp. 5030-5039
    • Olson, A.L.1    Eyster, C.A.2    Duggins, Q.S.3    Knight, J.B.4
  • 361
    • 84865182107 scopus 로고    scopus 로고
    • Sites of glucose transporter-4 vesicle fusion with the plasma membrane correlate spatially with microtubules
    • Dawicki-McKenna J.M., Goldman Y.E., Ostap E.M. Sites of glucose transporter-4 vesicle fusion with the plasma membrane correlate spatially with microtubules. PLoS One 2012, 7(8):e43662.
    • (2012) PLoS One , vol.7 , Issue.8
    • Dawicki-McKenna, J.M.1    Goldman, Y.E.2    Ostap, E.M.3
  • 362
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • Giorgino F., de Robertis O., Laviola L., Montrone C., Perrini S., McCowen K.C., et al. The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:1125-1130.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1125-1130
    • Giorgino, F.1    de Robertis, O.2    Laviola, L.3    Montrone, C.4    Perrini, S.5    McCowen, K.C.6
  • 363
    • 81155128125 scopus 로고    scopus 로고
    • GLUT4 and UBC9 protein expression is reduced in muscle from type 2 diabetic patients with severe insulin resistance
    • Kampmann U., Christensen B., Nielsen T.S., Pedersen S.B., Orskov L., Lund S., et al. GLUT4 and UBC9 protein expression is reduced in muscle from type 2 diabetic patients with severe insulin resistance. PLoS One 2011, 6(11):e27854.
    • (2011) PLoS One , vol.6 , Issue.11
    • Kampmann, U.1    Christensen, B.2    Nielsen, T.S.3    Pedersen, S.B.4    Orskov, L.5    Lund, S.6
  • 364
    • 84864975933 scopus 로고    scopus 로고
    • The Axin/TNKS complex interacts with KIF3A and is required for insulin-stimulated GLUT4 translocation
    • Guo H.L., Zhang C., Liu Q., Li Q., Lian G., Wu D., et al. The Axin/TNKS complex interacts with KIF3A and is required for insulin-stimulated GLUT4 translocation. Cell Res. 2012, 22(8):1246-1257.
    • (2012) Cell Res. , vol.22 , Issue.8 , pp. 1246-1257
    • Guo, H.L.1    Zhang, C.2    Liu, Q.3    Li, Q.4    Lian, G.5    Wu, D.6
  • 365
    • 0033580846 scopus 로고    scopus 로고
    • Aldolase mediates the association of F-actin with the insulin-responsive glucose transporter GLUT4
    • Kao A.W., Noda Y., Johnson J.H., Pessin J.E., Saltiel A.R. Aldolase mediates the association of F-actin with the insulin-responsive glucose transporter GLUT4. J. Biol. Chem. 1999, 274:17742-17747.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17742-17747
    • Kao, A.W.1    Noda, Y.2    Johnson, J.H.3    Pessin, J.E.4    Saltiel, A.R.5
  • 366
    • 2942537929 scopus 로고    scopus 로고
    • EHD2 interacts with the insulin-responsive glucose transporter (GLUT4) in rat adipocytes and may participate in insulin-induced GLUT4 recruitment
    • Park S.Y., Ha B.G., Choi G.H., Ryu J., Kim B., Jung C.Y., et al. EHD2 interacts with the insulin-responsive glucose transporter (GLUT4) in rat adipocytes and may participate in insulin-induced GLUT4 recruitment. Biochemistry 2004, 43(23):7552-7562.
    • (2004) Biochemistry , vol.43 , Issue.23 , pp. 7552-7562
    • Park, S.Y.1    Ha, B.G.2    Choi, G.H.3    Ryu, J.4    Kim, B.5    Jung, C.Y.6
  • 368
    • 0037205501 scopus 로고    scopus 로고
    • The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1
    • Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V. The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1. J. Biol. Chem. 2002, 277:19783-19791.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19783-19791
    • Lalioti, V.S.1    Vergarajauregui, S.2    Pulido, D.3    Sandoval, I.V.4
  • 369
    • 0028902985 scopus 로고
    • ATP-sensitive binding of a 70-kDa cytosolic protein to the glucose transporter in rat adipocytes
    • Liu H., Xiong S., Shi Y., Samuel S.J., Lachaal M., Jung C.Y. ATP-sensitive binding of a 70-kDa cytosolic protein to the glucose transporter in rat adipocytes. J. Biol. Chem. 1995, 270:7869-7875.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7869-7875
    • Liu, H.1    Xiong, S.2    Shi, Y.3    Samuel, S.J.4    Lachaal, M.5    Jung, C.Y.6
  • 370
    • 0344199888 scopus 로고    scopus 로고
    • Cloning of an L-3-hydroxyacyl-CoA dehydrogenase that interacts with the GLUT4 C-terminus
    • Shi Y., Samuel S.J., Lee W., Yu C., Zhang W., Lachaal M., et al. Cloning of an L-3-hydroxyacyl-CoA dehydrogenase that interacts with the GLUT4 C-terminus. Arch. Biochem. Biophys. 1999, 363:323-332.
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 323-332
    • Shi, Y.1    Samuel, S.J.2    Lee, W.3    Yu, C.4    Zhang, W.5    Lachaal, M.6
  • 372
    • 64249107656 scopus 로고    scopus 로고
    • GAPDH binds GLUT4 reciprocally to hexokinase-II and regulates glucose transport activity
    • Zaid H., Talior-Volodarsky I., Antonescu C., Liu Z., Klip A. GAPDH binds GLUT4 reciprocally to hexokinase-II and regulates glucose transport activity. Biochem. J. 2009, 419(2):475-484.
    • (2009) Biochem. J. , vol.419 , Issue.2 , pp. 475-484
    • Zaid, H.1    Talior-Volodarsky, I.2    Antonescu, C.3    Liu, Z.4    Klip, A.5
  • 374
    • 84863230479 scopus 로고    scopus 로고
    • The first luminal loop confers insulin responsiveness to glucose transporter 4
    • Kim J.Y., Kandror K.V. The first luminal loop confers insulin responsiveness to glucose transporter 4. Mol. Biol. Cell 2012, 23(5):910-917.
    • (2012) Mol. Biol. Cell , vol.23 , Issue.5 , pp. 910-917
    • Kim, J.Y.1    Kandror, K.V.2
  • 375
    • 0028211775 scopus 로고
    • The amino terminus of GLUT4 functions as an internalization motif but not an intracellular retention signal when substituted for the transferrin receptor cytoplasmic domain
    • Garippa R.J., Judge T.W., James D.E., McGraw T.E. The amino terminus of GLUT4 functions as an internalization motif but not an intracellular retention signal when substituted for the transferrin receptor cytoplasmic domain. J. Cell Biol. 1994, 124:705-715.
    • (1994) J. Cell Biol. , vol.124 , pp. 705-715
    • Garippa, R.J.1    Judge, T.W.2    James, D.E.3    McGraw, T.E.4
  • 376
    • 0033514292 scopus 로고    scopus 로고
    • Analysis of amino and carboxy terminal GLUT-4 targeting motifs in 3T3-L1 adipocytes using an endosomal ablation technique
    • Melvin D.R., Marsh B.J., Walmsley A.R., James D.E., Gould G.W. Analysis of amino and carboxy terminal GLUT-4 targeting motifs in 3T3-L1 adipocytes using an endosomal ablation technique. Biochemistry 1999, 38:1456-1462.
    • (1999) Biochemistry , vol.38 , pp. 1456-1462
    • Melvin, D.R.1    Marsh, B.J.2    Walmsley, A.R.3    James, D.E.4    Gould, G.W.5
  • 378
    • 0034071705 scopus 로고    scopus 로고
    • Intracellular targeting and retention of the glucose transporter GLUT4 by the perinuclear storage compartment involves distinct carboxyl-tail motifs
    • Martinez-Arca S., Lalioti V.S., Sandoval I.V. Intracellular targeting and retention of the glucose transporter GLUT4 by the perinuclear storage compartment involves distinct carboxyl-tail motifs. J. Cell Sci. 2000, 113:1705-1715.
    • (2000) J. Cell Sci. , vol.113 , pp. 1705-1715
    • Martinez-Arca, S.1    Lalioti, V.S.2    Sandoval, I.V.3
  • 379
    • 0029099399 scopus 로고
    • Distinct signals in the GLUT4 glucose transporter for internalization and for targeting to an insulin-responsive compartment
    • Verhey K.J., Yeh J.I., Birnbaum M.J. Distinct signals in the GLUT4 glucose transporter for internalization and for targeting to an insulin-responsive compartment. J. Cell Biol. 1995, 130:1071-1079.
    • (1995) J. Cell Biol. , vol.130 , pp. 1071-1079
    • Verhey, K.J.1    Yeh, J.I.2    Birnbaum, M.J.3
  • 380
    • 0034663471 scopus 로고    scopus 로고
    • The cytosolic C-terminus of the glucose transporter GLUT4 contains an acidic cluster endosomal targeting motif distal to the dileucine signal
    • Shewan A.M., Marsh B.J., Melvin D.R., Martin S., Gould G.W., James D.E. The cytosolic C-terminus of the glucose transporter GLUT4 contains an acidic cluster endosomal targeting motif distal to the dileucine signal. Biochem. J. 2000, 350:99-107.
    • (2000) Biochem. J. , vol.350 , pp. 99-107
    • Shewan, A.M.1    Marsh, B.J.2    Melvin, D.R.3    Martin, S.4    Gould, G.W.5    James, D.E.6
  • 381
    • 45549084383 scopus 로고    scopus 로고
    • Identification of amino acid residues within the C terminus of the GLUT4 glucose transporter that are essential for insulin-stimulated redistribution to the plasma membrane
    • Song X.M., Hresko R.C., Mueckler M. Identification of amino acid residues within the C terminus of the GLUT4 glucose transporter that are essential for insulin-stimulated redistribution to the plasma membrane. J. Biol. Chem. 2008, 283(18):12571-12585.
    • (2008) J. Biol. Chem. , vol.283 , Issue.18 , pp. 12571-12585
    • Song, X.M.1    Hresko, R.C.2    Mueckler, M.3


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