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Volumn 40, Issue 6, 2014, Pages 400-410

Molecular mechanisms of GLUT4 regulation in adipocytes

(1)  Govers, R a  

a INSERM   (France)

Author keywords

Adipocyte; GLUT4; Intracellular traffic; Regulated exocytosis; Translocation

Indexed keywords

GLUCOSE; GLUCOSE TRANSPORTER 4; INSULIN; INSULIN RECEPTOR; PHOSPHOLIPASE C; RAB PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN 2;

EID: 84919697366     PISSN: 12623636     EISSN: 18781780     Source Type: Journal    
DOI: 10.1016/j.diabet.2014.01.005     Document Type: Review
Times cited : (97)

References (147)
  • 1
    • 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, 57:693-705.
    • (1999) J Neurosci Res , vol.57 , pp. 693-705
    • Apelt, J.1    Mehlhorn, G.2    Schliebs, R.3
  • 2
    • 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, 42:1086-1092.
    • (1992) Kidney Int , vol.42 , pp. 1086-1092
    • Brosius, F.C.1    Briggs, J.P.2    Marcus, R.G.3    Barac-Nieto, M.4    Charron, M.J.5
  • 3
    • 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, 119:4686-4697.
    • (2012) Blood , vol.119 , 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
  • 4
    • 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, 144:4527-4535.
    • (2003) Endocrinology , vol.144 , pp. 4527-4535
    • Medina, R.A.1    Meneses, A.M.2    Vera, J.C.3    Guzman, C.4    Nualart, F.5    Astuya, A.6
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0036270751 scopus 로고    scopus 로고
    • Regulated transport of the glucose transporter GLUT4
    • Bryant N.J., Govers R., James D.E. Regulated transport of the glucose transporter GLUT4. Nat Rev Mol Cell Biol 2002, 3:267-277.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 267-277
    • Bryant, N.J.1    Govers, R.2    James, D.E.3
  • 9
    • 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
  • 10
    • 33947596679 scopus 로고    scopus 로고
    • The GLUT4 glucose transporter
    • Huang S., Czech M.P. The GLUT4 glucose transporter. Cell Metab 2007, 5:237-252.
    • (2007) Cell Metab , vol.5 , pp. 237-252
    • Huang, S.1    Czech, M.P.2
  • 11
    • 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, 42:1773-1785.
    • (1993) Diabetes , vol.42 , pp. 1773-1785
    • Garvey, W.T.1    Maianu, L.2    Zhu, J.H.3    Hancock, J.A.4    Golichowski, A.M.5
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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, 169:481-489.
    • (2005) J Cell Biol , vol.169 , pp. 481-489
    • Lizunov, V.A.1    Matsumoto, H.2    Zimmerberg, J.3    Cushman, S.W.4    Frolov, V.A.5
  • 17
    • 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, 5:19-27.
    • (1975) Cell , vol.5 , pp. 19-27
    • Green, H.1    Kehinde, O.2
  • 19
    • 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, 193:643-653.
    • (2011) J Cell Biol , vol.193 , pp. 643-653
    • Xu, Y.1    Rubin, B.R.2    Orme, C.M.3    Karpikov, A.4    Yu, C.5    Bogan, J.S.6
  • 20
    • 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
  • 21
    • 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, 21:2034-2044.
    • (2010) Mol Biol Cell , vol.21 , pp. 2034-2044
    • Jordens, I.1    Molle, D.2    Xiong, W.3    Keller, S.R.4    McGraw, T.E.5
  • 22
    • 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, 9:99-108.
    • (2005) Dev Cell , vol.9 , pp. 99-108
    • Shi, J.1    Kandror, K.V.2
  • 23
    • 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, 285:104-114.
    • (2010) J Biol Chem , vol.285 , 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
  • 24
    • 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, 280:37803-37813.
    • (2005) J Biol Chem , vol.280 , pp. 37803-37813
    • Larance, M.1    Ramm, G.2    Stockli, J.3    van Dam, E.M.4    Winata, S.5    Wasinger, V.6
  • 25
    • 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
  • 26
    • 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, 283:30311-30321.
    • (2008) J Biol Chem , vol.283 , pp. 30311-30321
    • Shi, J.1    Huang, G.2    Kandror, K.V.3
  • 27
    • 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, 52:932-940.
    • (2009) Diabetologia , vol.52 , pp. 932-940
    • Kaddai, V.1    Jager, J.2    Gonzalez, T.3    Najem-Lendom, R.4    Bonnafous, S.5    Tran, A.6
  • 28
    • 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, 285:34371-34381.
    • (2010) J Biol Chem , vol.285 , pp. 34371-34381
    • Tsuchiya, Y.1    Hatakeyama, H.2    Emoto, N.3    Wagatsuma, F.4    Matsushita, S.5    Kanzaki, M.6
  • 29
    • 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, 282:9008-9016.
    • (2007) J Biol Chem , vol.282 , pp. 9008-9016
    • Shi, J.1    Kandror, K.V.2
  • 30
    • 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, 21:1375-1386.
    • (2010) Mol Biol Cell , vol.21 , pp. 1375-1386
    • Xiong, W.1    Jordens, I.2    Gonzalez, E.3    McGraw, T.E.4
  • 31
    • 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, 277:17677-17686.
    • (2002) J Biol Chem , vol.277 , pp. 17677-17686
    • Keller, S.R.1    Davis, A.C.2    Clairmont, K.B.3
  • 32
    • 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, 203:537-550.
    • (2013) J Cell Biol , vol.203 , pp. 537-550
    • Briguglio, J.S.1    Kumar, S.2    Turkewitz, A.P.3
  • 33
    • 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, 2:179-189.
    • (2005) Cell Metab , vol.2 , pp. 179-189
    • Koumanov, F.1    Jin, B.2    Yang, J.3    Holman, G.D.4
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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, 287:23932-23947.
    • (2012) J Biol Chem , vol.287 , 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
  • 37
    • 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, 287:6679-6692.
    • (2012) J Biol Chem , vol.287 , pp. 6679-6692
    • Orme, C.M.1    Bogan, J.S.2
  • 38
    • 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, 17:5346-5355.
    • (2006) Mol Biol Cell , vol.17 , pp. 5346-5355
    • Williams, D.1    Hicks, S.W.2    Machamer, C.E.3    Pessin, J.E.4
  • 39
    • 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, 282:7710-7722.
    • (2007) J Biol Chem , vol.282 , pp. 7710-7722
    • Yu, C.1    Cresswell, J.2    Loffler, M.G.3    Bogan, J.S.4
  • 40
  • 41
    • 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
  • 42
    • 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, 198:545-560.
    • (2012) J Cell Biol , vol.198 , pp. 545-560
    • Chen, Y.1    Wang, Y.2    Zhang, J.3    Deng, Y.4    Jiang, L.5    Song, E.6
  • 43
    • 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
  • 44
    • 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, 283:311-323.
    • (2008) J Biol Chem , vol.283 , pp. 311-323
    • Muretta, J.M.1    Romenskaia, I.2    Mastick, C.C.3
  • 45
    • 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, 19:3477-3487.
    • (2008) Mol Biol Cell , vol.19 , pp. 3477-3487
    • Blot, V.1    McGraw, T.E.2
  • 46
    • 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
  • 47
    • 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
  • 48
    • 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, 445:265-273.
    • (2012) Biochem J , vol.445 , pp. 265-273
    • Zaarour, N.1    Berenguer, M.2    Le Marchand-Brustel, Y.3    Govers, R.4
  • 49
    • 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
  • 50
    • 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, 584:537-542.
    • (2010) FEBS Lett , vol.584 , pp. 537-542
    • Berenguer, M.1    Le Marchand-Brustel, Y.2    Govers, R.3
  • 51
    • 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
  • 52
    • 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
  • 53
    • 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
  • 55
    • 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, 6:1142-1156.
    • (2005) Traffic , vol.6 , pp. 1142-1156
    • Lock, J.G.1    Hammond, L.A.2    Houghton, F.3    Gleeson, P.A.4    Stow, J.L.5
  • 56
    • 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, 124:735-744.
    • (2011) J Cell Sci , vol.124 , pp. 735-744
    • Park, J.J.1    Gondre-Lewis, M.C.2    Eiden, L.E.3    Loh, Y.P.4
  • 57
    • 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
  • 58
    • 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
  • 59
    • 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, 23:2059-2070.
    • (2004) Embo J , vol.23 , pp. 2059-2070
    • Watson, R.T.1    Khan, A.H.2    Furukawa, M.3    Hou, J.C.4    Li, L.5    Kanzaki, M.6
  • 60
    • 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, 19:2145-2153.
    • (2005) Mol Endocrinol , vol.19 , pp. 2145-2153
    • Li, L.V.1    Kandror, K.V.2
  • 61
    • 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, 12:1805-1820.
    • (2011) Traffic , vol.12 , pp. 1805-1820
    • Hatakeyama, H.1    Kanzaki, M.2
  • 62
    • 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, 16:2882-2890.
    • (2005) Mol Biol Cell , vol.16 , pp. 2882-2890
    • Hosaka, T.1    Brooks, C.C.2    Presman, E.3    Kim, S.K.4    Zhang, Z.5    Breen, M.6
  • 63
    • 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, 402:279-290.
    • (2007) Biochem J , vol.402 , pp. 279-290
    • Yeh, T.Y.1    Sbodio, J.I.2    Tsun, Z.Y.3    Luo, B.4    Chi, N.W.5
  • 64
    • 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, 324:1192-1196.
    • (2009) Science , vol.324 , pp. 1192-1196
    • Vassilopoulos, S.1    Esk, C.2    Hoshino, S.3    Funke, B.H.4    Chen, C.Y.5    Plocik, A.M.6
  • 65
    • 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, 188:131-144.
    • (2010) J Cell Biol , vol.188 , pp. 131-144
    • Esk, C.1    Chen, C.Y.2    Johannes, L.3    Brodsky, F.M.4
  • 66
    • 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
  • 67
    • 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, 21:2721-2731.
    • (2010) Mol Biol Cell , vol.21 , pp. 2721-2731
    • Fujita, H.1    Hatakeyama, H.2    Watanabe, T.M.3    Sato, M.4    Higuchi, H.5    Kanzaki, M.6
  • 68
    • 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, 27:3456-3469.
    • (2007) Mol Cell Biol , vol.27 , pp. 3456-3469
    • Huang, S.1    Lifshitz, L.M.2    Jones, C.3    Bellve, K.D.4    Standley, C.5    Fonseca, S.6
  • 69
    • 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, 283:8508-8516.
    • (2008) J Biol Chem , vol.283 , pp. 8508-8516
    • Jiang, L.1    Fan, J.2    Bai, L.3    Wang, Y.4    Chen, Y.5    Yang, L.6
  • 70
    • 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, 5:47-57.
    • (2007) Cell Metab , vol.5 , pp. 47-57
    • Bai, L.1    Wang, Y.2    Fan, J.3    Chen, Y.4    Ji, W.5    Qu, A.6
  • 71
  • 72
    • 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
  • 73
    • 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
  • 74
    • 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
  • 75
    • 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
  • 76
    • 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, 25:5648-5658.
    • (2006) Embo J , vol.25 , pp. 5648-5658
    • Blot, V.1    McGraw, T.E.2
  • 78
    • 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, 12:250-259.
    • (2010) Cell Metab , vol.12 , pp. 250-259
    • Stenkula, K.G.1    Lizunov, V.A.2    Cushman, S.W.3    Zimmerberg, J.4
  • 79
    • 84874781879 scopus 로고    scopus 로고
    • Insulin regulates Glut4 confinement in plasma membrane clusters in adipose cells
    • Lizunov V.A., Stenkula K., Troy A., Cushman S.W., Zimmerberg J. Insulin regulates Glut4 confinement in plasma membrane clusters in adipose cells. PLoS One 2013, 8:e57559.
    • (2013) PLoS One , vol.8 , pp. e57559
    • Lizunov, V.A.1    Stenkula, K.2    Troy, A.3    Cushman, S.W.4    Zimmerberg, J.5
  • 80
    • 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
  • 81
    • 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
  • 82
    • 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
  • 83
    • 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, 7:348-356.
    • (2008) Cell Metab , vol.7 , pp. 348-356
    • Ng, Y.1    Ramm, G.2    Lopez, J.A.3    James, D.E.4
  • 84
    • 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, 17:4484-4493.
    • (2006) Mol Biol Cell , vol.17 , pp. 4484-4493
    • Gonzalez, E.1    McGraw, T.E.2
  • 85
    • 0031724590 scopus 로고    scopus 로고
    • Requirement of atypical protein kinase C-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 C-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
  • 86
    • 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
  • 87
    • 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
  • 88
    • 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(Pt 3):461-470.
    • (1999) Biochem J , vol.337 , pp. 461-470
    • Bandyopadhyay, G.1    Standaert, M.L.2    Kikkawa, U.3    Ono, Y.4    Moscat, J.5    Farese, R.V.6
  • 89
    • 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, 273:13808-13818.
    • (1998) J Biol Chem , vol.273 , pp. 13808-13818
    • Kayali, A.G.1    Eichhorn, J.2    Haruta, T.3    Morris, A.J.4    Nelson, J.G.5    Vollenweider, P.6
  • 90
    • 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
  • 91
    • 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
  • 92
    • 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, 148:27-33.
    • (2007) Endocrinology , vol.148 , pp. 27-33
    • Chang, L.1    Chiang, S.H.2    Saltiel, A.R.3
  • 93
    • 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, 283:35455-35463.
    • (2008) J Biol Chem , vol.283 , pp. 35455-35463
    • Okada, S.1    Yamada, E.2    Saito, T.3    Ohshima, K.4    Hashimoto, K.5    Yamada, M.6
  • 94
    • 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, 22:3599-3609.
    • (2002) Mol Cell Biol , vol.22 , pp. 3599-3609
    • Liu, J.1    Kimura, A.2    Baumann, C.A.3    Saltiel, A.R.4
  • 95
    • 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
  • 96
    • 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, 279:37431-37435.
    • (2004) J Biol Chem , vol.279 , pp. 37431-37435
    • Mitra, P.1    Zheng, X.2    Czech, M.P.3
  • 97
    • 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, 284:7914-7919.
    • (2009) J Biol Chem , vol.284 , pp. 7914-7919
    • Lizunov, V.A.1    Lisinski, I.2    Stenkula, K.3    Zimmerberg, J.4    Cushman, S.W.5
  • 98
    • 79952107840 scopus 로고    scopus 로고
    • Signaling, cytoskeletal and membrane mechanisms regulating GLUT4 exocytosis
    • Hoffman N.J., Elmendorf J.S. Signaling, cytoskeletal and membrane mechanisms regulating GLUT4 exocytosis. Trends Endocrinol Metab 2011, 22:110-116.
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 110-116
    • Hoffman, N.J.1    Elmendorf, J.S.2
  • 99
    • 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, 271:665-668.
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 100
    • 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, 57:2644-2651.
    • (2008) Diabetes , vol.57 , pp. 2644-2651
    • Morino, K.1    Neschen, S.2    Bilz, S.3    Sono, S.4    Tsirigotis, D.5    Reznick, R.M.6
  • 101
    • 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, 50:2563-2571.
    • (2001) Diabetes , vol.50 , pp. 2563-2571
    • Teruel, T.1    Hernandez, R.2    Lorenzo, M.3
  • 102
    • 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, 56:875-885.
    • (2013) Diabetologia , vol.56 , 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
  • 103
    • 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, 285:5232-5239.
    • (2010) J Biol Chem , vol.285 , pp. 5232-5239
    • Ng, Y.1    Ramm, G.2    James, D.E.3
  • 104
    • 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, 342:751-757.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 751-757
    • Gupte, A.1    Mora, S.2
  • 105
    • 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 (Silver Spring) 2008, 16:1226-1231.
    • (2008) Obesity (Silver Spring) , vol.16 , pp. 1226-1231
    • Jun, H.S.1    Hwang, K.2    Kim, Y.3    Park, T.4
  • 106
    • 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
  • 107
    • 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:E1273-E1286.
    • (2012) Am J Physiol Endocrinol Metab , vol.303 , pp. E1273-E1286
    • Lansey, M.N.1    Walker, N.N.2    Hargett, S.R.3    Stevens, J.R.4    Keller, S.R.5
  • 108
    • 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, 391:87-93.
    • (2005) Biochem J , vol.391 , pp. 87-93
    • Miinea, C.P.1    Sano, H.2    Kane, S.3    Sano, E.4    Fukuda, M.5    Peranen, J.6
  • 109
    • 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
  • 110
    • 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, 287:26890-26900.
    • (2012) J Biol Chem , vol.287 , pp. 26890-26900
    • Ren, W.1    Cheema, S.2    Du, K.3
  • 111
    • 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, 2:263-272.
    • (2005) Cell Metab , vol.2 , pp. 263-272
    • Eguez, L.1    Lee, A.2    Chavez, J.A.3    Miinea, C.P.4    Kane, S.5    Lienhard, G.E.6
  • 112
    • 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, 286:26287-26297.
    • (2011) J Biol Chem , vol.286 , pp. 26287-26297
    • Brewer, P.D.1    Romenskaia, I.2    Kanow, M.A.3    Mastick, C.C.4
  • 113
    • 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, 32:4946-4959.
    • (2012) Mol Cell Biol , vol.32 , pp. 4946-4959
    • Tan, S.X.1    Ng, Y.2    Burchfield, J.G.3    Ramm, G.4    Lambright, D.G.5    Stockli, J.6
  • 114
    • 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, 24:2544-2557.
    • (2013) Mol Biol Cell , vol.24 , pp. 2544-2557
    • Sadacca, L.A.1    Bruno, J.2    Wen, J.3    Xiong, W.4    McGraw, T.E.5
  • 115
    • 34447499043 scopus 로고    scopus 로고
    • Myosin 5a is an insulin-stimulated Akt2 (protein kinase Bbeta) 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 Bbeta) substrate modulating GLUT4 vesicle translocation. Mol Cell Biol 2007, 27:5172-5183.
    • (2007) Mol Cell Biol , vol.27 , pp. 5172-5183
    • Yoshizaki, T.1    Imamura, T.2    Babendure, J.L.3    Lu, J.C.4    Sonoda, N.5    Olefsky, J.M.6
  • 116
    • 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, 22:1286-1298.
    • (2012) Dev Cell , vol.22 , pp. 1286-1298
    • Li, J.1    Malaby, A.W.2    Famulok, M.3    Sabe, H.4    Lambright, D.G.5    Hsu, V.W.6
  • 117
    • 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
  • 118
    • 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, 14:378-389.
    • (2011) Cell Metab , vol.14 , pp. 378-389
    • Xie, X.1    Gong, Z.2    Mansuy-Aubert, V.3    Zhou, Q.L.4    Tatulian, S.A.5    Sehrt, D.6
  • 119
    • 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
  • 121
    • 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, 168:921-928.
    • (2005) J Cell Biol , vol.168 , pp. 921-928
    • Yamada, E.1    Okada, S.2    Saito, T.3    Ohshima, K.4    Sato, M.5    Tsuchiya, T.6
  • 122
    • 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, 117:5985-5993.
    • (2004) J Cell Sci , vol.117 , 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
  • 123
    • 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, 5:293-303.
    • (2007) Cell Metab , vol.5 , pp. 293-303
    • Sano, H.1    Eguez, L.2    Teruel, M.N.3    Fukuda, M.4    Chuang, T.D.5    Chavez, J.A.6
  • 125
    • 84879071925 scopus 로고    scopus 로고
    • Rab10 delivers GLUT4 storage vesicles to the plasma membrane
    • Chen Y., Lippincott-Schwartz J. Rab10 delivers GLUT4 storage vesicles to the plasma membrane. Commun Integr Biol 2013, 6:e23779.
    • (2013) Commun Integr Biol , vol.6 , pp. e23779
    • Chen, Y.1    Lippincott-Schwartz, J.2
  • 126
    • 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, 286:16541-16545.
    • (2011) J Biol Chem , vol.286 , pp. 16541-16545
    • Sano, H.1    Peck, G.R.2    Kettenbach, A.N.3    Gerber, S.A.4    Lienhard, G.E.5
  • 127
    • 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, 126:1931-1941.
    • (2013) J Cell Sci , vol.126 , 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
  • 128
    • 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, 5:59-72.
    • (2007) Cell Metab , vol.5 , pp. 59-72
    • Lodhi, I.J.1    Chiang, S.H.2    Chang, L.3    Vollenweider, D.4    Watson, R.T.5    Inoue, M.6
  • 129
    • 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
  • 131
    • 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:R517-R531.
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.298 , pp. R517-R531
    • Jewell, J.L.1    Oh, E.2    Thurmond, D.C.3
  • 132
    • 0030464997 scopus 로고    scopus 로고
    • Insulin-stimulated translocation of GLUT4 glucose transporters requires SNARE-complex proteins
    • Cheatham B., Volchuk A., Kahn C.R., Wang L., Rhodes C.J., Klip A. Insulin-stimulated translocation of GLUT4 glucose transporters requires SNARE-complex proteins. Proc Natl Acad Sci U S A 1996, 93:15169-15173.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 15169-15173
    • Cheatham, B.1    Volchuk, A.2    Kahn, C.R.3    Wang, L.4    Rhodes, C.J.5    Klip, A.6
  • 133
    • 0030917678 scopus 로고    scopus 로고
    • Functional studies in 3T3-L1 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 3T3-L1 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
  • 134
    • 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
  • 135
    • 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, 122:3472-3480.
    • (2009) J Cell Sci , vol.122 , pp. 3472-3480
    • Zhao, P.1    Yang, L.2    Lopez, J.A.3    Fan, J.4    Burchfield, J.G.5    Bai, L.6
  • 136
    • 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, 24:1176-1184.
    • (2013) Mol Biol Cell , vol.24 , pp. 1176-1184
    • Yu, H.1    Rathore, S.S.2    Davis, E.M.3    Ouyang, Y.4    Shen, J.5
  • 138
    • 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, 347:433-438.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 433-438
    • Proctor, K.M.1    Miller, S.C.2    Bryant, N.J.3    Gould, G.W.4
  • 139
    • 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
  • 140
    • 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, 24:2389-2397.
    • (2013) Mol Biol Cell , vol.24 , pp. 2389-2397
    • Roccisana, J.1    Sadler, J.B.2    Bryant, N.J.3    Gould, G.W.4
  • 141
    • 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
  • 142
    • 0032509214 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated GLUT4 translocation by Munc18c in 3T3-L1 adipocytes
    • Thurmond D.C., Ceresa B.P., Okada S., Elmendorf J.S., Coker K., Pessin J.E. Regulation of insulin-stimulated GLUT4 translocation by Munc18c in 3T3-L1 adipocytes. J Biol Chem 1998, 273:33876-33883.
    • (1998) J Biol Chem , vol.273 , pp. 33876-33883
    • Thurmond, D.C.1    Ceresa, B.P.2    Okada, S.3    Elmendorf, J.S.4    Coker, K.5    Pessin, J.E.6
  • 143
    • 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, 55:2171-2179.
    • (2006) Diabetes , vol.55 , pp. 2171-2179
    • Schmelzle, K.1    Kane, S.2    Gridley, S.3    Lienhard, G.E.4    White, F.M.5
  • 144
    • 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, 193:185-199.
    • (2011) J Cell Biol , vol.193 , pp. 185-199
    • Jewell, J.L.1    Oh, E.2    Ramalingam, L.3    Kalwat, M.A.4    Tagliabracci, V.S.5    Tackett, L.6
  • 145
    • 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, 115:291-301.
    • (2005) J Clin Invest , vol.115 , pp. 291-301
    • Kanda, H.1    Tamori, Y.2    Shinoda, H.3    Yoshikawa, M.4    Sakaue, M.5    Udagawa, J.6
  • 146
    • 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
  • 147
    • 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, 58:377-384.
    • (2009) Diabetes , vol.58 , pp. 377-384
    • Fukuda, N.1    Emoto, M.2    Nakamori, Y.3    Taguchi, A.4    Miyamoto, S.5    Uraki, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.