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Volumn 18, Issue 5, 2002, Pages 345-356

An adipocentric view of signaling and intracellular trafficking

Author keywords

Adipocytes; Endocrine tissue; Hormones; Secretion; Trafficking

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; ACYLATION STIMULATING PROTEIN; ADIPONECTIN; ADIPSIN; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; BREFELDIN A; CYCLOHEXIMIDE; FATTY ACID; GLUCOSE TRANSPORTER 4; INSULIN; INTERLEUKIN 6; LEPTIN; LIPOPROTEIN LIPASE; RAPAMYCIN; RESISTIN; TRIACYLGLYCEROL; TUMOR NECROSIS FACTOR ALPHA; VASCULOTROPIN;

EID: 0036710513     PISSN: 15207552     EISSN: None     Source Type: Journal    
DOI: 10.1002/dmrr.321     Document Type: Review
Times cited : (154)

References (174)
  • 1
    • 0032558725 scopus 로고    scopus 로고
    • Leptin and the regulation of body weight in mammals
    • Friedman J, Halaas J. Leptin and the regulation of body weight in mammals. Nature 1998; 395: 763-770.
    • (1998) Nature , vol.395 , pp. 763-770
    • Friedman, J.1    Halaas, J.2
  • 2
    • 0029131574 scopus 로고
    • Expression of ob mRNA and its encoded protein in rodents. Impact of nutrition and obesity
    • Frederich R, Hamann A, Anderson S, Lollmann B, Lowell B, Flier J. Expression of ob mRNA and its encoded protein in rodents. Impact of nutrition and obesity. J Clin Invest 1995; 96: 1658-1663.
    • (1995) J. Clin. Invest , vol.96 , pp. 1658-1663
    • Frederich, R.1    Hamann, A.2    Anderson, S.3    Lollmann, B.4    Lowell, B.5    Flier, J.6
  • 3
    • 0029102059 scopus 로고
    • Modulation of obese gene expression in rat brown and white adipose tissues
    • Moinat M, Deng C, Muzzin P, et al. Modulation of obese gene expression in rat brown and white adipose tissues. FEBS Lett 1995; 373: 131-134.
    • (1995) FEBS Lett , vol.373 , pp. 131-134
    • Moinat, M.1    Deng, C.2    Muzzin, P.3
  • 4
    • 0031039824 scopus 로고    scopus 로고
    • Effects of beta-adrenoceptory subtype stimulation on obese gene messenger ribonucleic acid and on leptin secretion in mouse brown adipocytes differentiated in culture
    • Deng C, Moinat M, Curtis L, et al. Effects of beta-adrenoceptory subtype stimulation on obese gene messenger ribonucleic acid and on leptin secretion in mouse brown adipocytes differentiated in culture. Endocrinology 1997; 138: 548-552.
    • (1997) Endocrinology , vol.138 , pp. 548-552
    • Deng, C.1    Moinat, M.2    Curtis, L.3
  • 5
    • 0033930048 scopus 로고    scopus 로고
    • Leptin secretion and leptin receptor in the human stomach
    • Sobhani I, Bado A, Vissuzaine C, et al. Leptin secretion and leptin receptor in the human stomach. Gut 2000; 47: 178-183.
    • (2000) Gut , vol.47 , pp. 178-183
    • Sobhani, I.1    Bado, A.2    Vissuzaine, C.3
  • 6
    • 0032552112 scopus 로고    scopus 로고
    • The stomach is a source of leptin
    • Bado A, Levasseur S, Attoub S, et al. The stomach is a source of leptin. Nature 1998; 394: 790-793.
    • (1998) Nature , vol.394 , pp. 790-793
    • Bado, A.1    Levasseur, S.2    Attoub, S.3
  • 8
    • 0034951972 scopus 로고    scopus 로고
    • Leptin expression in placental and fetal tissues: Does leptin have a functional role?
    • Hoggard N, Haggarty P, Thomas L, Lea R. Leptin expression in placental and fetal tissues: Does leptin have a functional role? Biochem Soc Trans 2001; 29: 57-63.
    • (2001) Biochem. Soc. Trans , vol.29 , pp. 57-63
    • Hoggard, N.1    Haggarty, P.2    Thomas, L.3    Lea, R.4
  • 9
    • 0032543680 scopus 로고    scopus 로고
    • A nutrient-sensing pathway regulates leptin gene expression in muscle and fat
    • Wang J, Liu R, Hawkins M, Barzilai N, Rossetti L. A nutrient-sensing pathway regulates leptin gene expression in muscle and fat. Nature 1998; 393: 684-688.
    • (1998) Nature , vol.393 , pp. 684-688
    • Wang, J.1    Liu, R.2    Hawkins, M.3    Barzilai, N.4    Rossetti, L.5
  • 11
    • 2442654859 scopus 로고
    • Identification and expression cloning of a leptin receptor, OB-R
    • Tartaglia L, Dembski M, Weng X, et al. Identification and expression cloning of a leptin receptor, OB-R. Cell 1995; 83: 1263-1271.
    • (1995) Cell , vol.83 , pp. 1263-1271
    • Tartaglia, L.1    Dembski, M.2    Weng, X.3
  • 12
    • 0028825577 scopus 로고
    • Recombinant ob protein reduces feeding and body weight in the ob/ob mouse
    • Weigle D, Bukowski T, Foster D, et al. Recombinant ob protein reduces feeding and body weight in the ob/ob mouse. J Clin Invest 1995; 96: 2065-2070.
    • (1995) J. Clin. Invest , vol.96 , pp. 2065-2070
    • Weigle, D.1    Bukowski, T.2    Foster, D.3
  • 13
    • 0029073613 scopus 로고
    • Weight-reducing effects of the plasma protein encoded by the obese gene
    • Halaas J, Gajiwala K, Maffei M, et al. Weight-reducing effects of the plasma protein encoded by the obese gene. Science 1995; 269: 543-546.
    • (1995) Science , vol.269 , pp. 543-546
    • Halaas, J.1    Gajiwala, K.2    Maffei, M.3
  • 14
    • 0029048408 scopus 로고
    • Recombinant mouse OB protein: Evidence for a peripheral signal linking adiposity and central neural networks
    • Campfield L, Smith F, Guisez Y, Devos R, Burn P. Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks. Science 1995; 269: 546-549.
    • (1995) Science , vol.269 , pp. 546-549
    • Campfield, L.1    Smith, F.2    Guisez, Y.3    Devos, R.4    Burn, P.5
  • 15
    • 0030847432 scopus 로고    scopus 로고
    • Acute stimulation of glucose metabolism in mice by leptin treatment
    • Kamohara S, Burcelin R, Halaas J, Friedman J, Charron M. Acute stimulation of glucose metabolism in mice by leptin treatment. Nature 1997; 389: 374-377.
    • (1997) Nature , vol.389 , pp. 374-377
    • Kamohara, S.1    Burcelin, R.2    Halaas, J.3    Friedman, J.4    Charron, M.5
  • 16
    • 0032572722 scopus 로고    scopus 로고
    • Leptin modulates the T-cell immune response and reverses starvation-induced immunosuppression
    • Lord G, Matarese G, Howard J, Baker R, Bloom S, Lechler R. Leptin modulates the T-cell immune response and reverses starvation-induced immunosuppression. Nature 1998; 394: 897-901.
    • (1998) Nature , vol.394 , pp. 897-901
    • Lord, G.1    Matarese, G.2    Howard, J.3    Baker, R.4    Bloom, S.5    Lechler, R.6
  • 17
    • 0030010388 scopus 로고    scopus 로고
    • Correction of the sterility defect in homozygous obese female mice by treatment with the human recombinant leptin
    • Chehab F, Lim M, Lu R. Correction of the sterility defect in homozygous obese female mice by treatment with the human recombinant leptin. Nat Genet 1996; 12: 318-320.
    • (1996) Nat. Genet , vol.12 , pp. 318-320
    • Chehab, F.1    Lim, M.2    Lu, R.3
  • 18
    • 0031014413 scopus 로고    scopus 로고
    • Early onset of reproductive function in normal female mice treated with leptin
    • Chehab F, Mounzih K, Lu R, Lim M. Early onset of reproductive function in normal female mice treated with leptin. Science 1997; 275: 88-90.
    • (1997) Science , vol.275 , pp. 88-90
    • Chehab, F.1    Mounzih, K.2    Lu, R.3    Lim, M.4
  • 21
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    • Minokoshi Y, Kim Y, Peroni O, et al. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 2002; 415: 339-343.
    • (2002) Nature , vol.415 , pp. 339-343
    • Minokoshi, Y.1    Kim, Y.2    Peroni, O.3
  • 22
    • 0035125097 scopus 로고    scopus 로고
    • Physiological increase in plasma leptin markedly inhibits insulin secretion in vivo
    • Cases AJ, Gabriely I, Hiu Ma X, et al. Physiological increase in plasma leptin markedly inhibits insulin secretion in vivo. Diabetes 2001; 50: 348-352.
    • (2001) Diabetes , vol.50 , pp. 348-352
    • Cases, A.J.1    Gabriely, I.2    Hiu Ma, X.3
  • 23
    • 0034881391 scopus 로고    scopus 로고
    • The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
    • Berg A, Combs T, Du X, Brownlee M, Scherer P. The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nat Med 2001; 7: 847-853.
    • (2001) Nat. Med , vol.7 , pp. 847-853
    • Berg, A.1    Combs, T.2    Du, X.3    Brownlee, M.4    Scherer, P.5
  • 24
    • 0035663963 scopus 로고    scopus 로고
    • Endogenous glucose production is inhibited by the adipose-derived protein ACRP30
    • Combs TP, Berg AH, Obici S, Scherer PE, Rossetti L. Endogenous glucose production is inhibited by the adipose-derived protein ACRP30. J Clin Invest 2001; 108: 1875-1881.
    • (2001) J. Clin. Invest , vol.108 , pp. 1875-1881
    • Combs, T.P.1    Berg, A.H.2    Obici, S.3    Scherer, P.E.4    Rossetti, L.5
  • 25
    • 17944365228 scopus 로고    scopus 로고
    • The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity
    • Yamauchi T, Kamon J, Waki H, et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat Med 2001; 7: 941-946.
    • (2001) Nat. Med , vol.7 , pp. 941-946
    • Yamauchi, T.1    Kamon, J.2    Waki, H.3
  • 26
    • 0035852760 scopus 로고    scopus 로고
    • Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice
    • Fruebis J, Tsao T, Javorschi S, et al. Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc Natl Acad Sci USA 2001; 98: 2005-2010.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2005-2010
    • Fruebis, J.1    Tsao, T.2    Javorschi, S.3
  • 27
    • 0030039272 scopus 로고    scopus 로고
    • Abnormal splicing of the leptin receptor in diabetic mice
    • Lee G, Proenca R, Montez J, et al. Abnormal splicing of the leptin receptor in diabetic mice. Nature 1996; 379: 632-635.
    • (1996) Nature , vol.379 , pp. 632-635
    • Lee, G.1    Proenca, R.2    Montez, J.3
  • 29
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman LD, Boss O, Peroni OD, et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol Cell Biol 2000; 15: 5479-5489.
    • (2000) Mol. Cell. Biol , vol.15 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3
  • 31
    • 0036228770 scopus 로고    scopus 로고
    • Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B
    • Cheng A, Uetani N, Simoncic PD, et al. Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B. Dev Cell 2002; 2: 497-503.
    • (2002) Dev. Cell , vol.2 , pp. 497-503
    • Cheng, A.1    Uetani, N.2    Simoncic, P.D.3
  • 32
    • 0033969577 scopus 로고    scopus 로고
    • Tumour necrosis factor-alpha exerts dual effects on human adipose leptin synthesis and release
    • Zhang H, Kumar S, Barnett A, Eggo M. Tumour necrosis factor-alpha exerts dual effects on human adipose leptin synthesis and release. Mol Cell Endocrinol 2000; 159: 79-88.
    • (2000) Mol. Cell. Endocrinol , vol.159 , pp. 79-88
    • Zhang, H.1    Kumar, S.2    Barnett, A.3    Eggo, M.4
  • 33
    • 0029157428 scopus 로고
    • Transient increase in obese gene expression after food intake or insulin administration
    • Saladin R, De Vos P, Guerre-Millo M, et al. Transient increase in obese gene expression after food intake or insulin administration. Nature 1995; 377: 527-529.
    • (1995) Nature , vol.377 , pp. 527-529
    • Saladin, R.1    De Vos, P.2    Guerre-Millo, M.3
  • 34
    • 0030455365 scopus 로고    scopus 로고
    • Regulation of leptin production in cultured mature white adipocytes
    • Hardie L, Guilhot N, Trayhurn P. Regulation of leptin production in cultured mature white adipocytes. Horm Metab Res 1996; 28: 685-689.
    • (1996) Horm. Metab. Res , vol.28 , pp. 685-689
    • Hardie, L.1    Guilhot, N.2    Trayhurn, P.3
  • 35
    • 0032969115 scopus 로고    scopus 로고
    • Regulation of ob gene expression and leptin secretion by insulin and dexamethasone in rat adipocytes
    • Bradley R, Cheatham B. Regulation of ob gene expression and leptin secretion by insulin and dexamethasone in rat adipocytes. Diabetes 1999; 48: 272-279.
    • (1999) Diabetes , vol.48 , pp. 272-279
    • Bradley, R.1    Cheatham, B.2
  • 36
    • 0030481888 scopus 로고    scopus 로고
    • High leptin concentrations in serum of very obese children are further stimulated by dexamethasone
    • Kiess W, Englaro P, Hanitsch S, Rascher W, Attanasio A, Blum W. High leptin concentrations in serum of very obese children are further stimulated by dexamethasone. Horm Metab Res 1996; 28: 708-710.
    • (1996) Horm. Metab. Res , vol.28 , pp. 708-710
    • Kiess, W.1    Englaro, P.2    Hanitsch, S.3    Rascher, W.4    Attanasio, A.5    Blum, W.6
  • 38
    • 0031762372 scopus 로고    scopus 로고
    • Multihormonal control of ob gene expression and leptin secretion from cultured human visceral adipose tissue: Increased responsiveness to glucocorticoids in obesity
    • Halleux C, Servais I, Reul B, Detry R, Brichard S. Multihormonal control of ob gene expression and leptin secretion from cultured human visceral adipose tissue: increased responsiveness to glucocorticoids in obesity. J Clin Endocrinol Metab 1998; 83: 902-910.
    • (1998) J. Clin. Endocrinol. Metab , vol.83 , pp. 902-910
    • Halleux, C.1    Servais, I.2    Reul, B.3    Detry, R.4    Brichard, S.5
  • 39
    • 0000113890 scopus 로고    scopus 로고
    • Thiazolidinediones repress ob gene expression in rodents via activation of peroxisome proliferator-activated receptor gamma
    • De Vos P, Lefebvre A, Miller S, et al. Thiazolidinediones repress ob gene expression in rodents via activation of peroxisome proliferator-activated receptor gamma. J Clin Invest 1996; 98: 1004-1009.
    • (1996) J. Clin. Invest , vol.98 , pp. 1004-1009
    • De Vos, P.1    Lefebvre, A.2    Miller, S.3
  • 41
    • 0032739022 scopus 로고    scopus 로고
    • Neuroendocrine regulation and actions of leptin
    • Casanueva F, Dieguez C. Neuroendocrine regulation and actions of leptin. Front Neuroendocrinol 1999; 20: 317-363.
    • (1999) Front. Neuroendocrinol , vol.20 , pp. 317-363
    • Casanueva, F.1    Dieguez, C.2
  • 42
    • 0030928781 scopus 로고    scopus 로고
    • Insulin stimulates both leptin secretion and production by rat white adipose tissue
    • Barr V, Malide D, Zarnowski M, Taylor S, Cushman S. Insulin stimulates both leptin secretion and production by rat white adipose tissue. Endocrinology 1997; 138: 4463-4472.
    • (1997) Endocrinology , vol.138 , pp. 4463-4472
    • Barr, V.1    Malide, D.2    Zarnowski, M.3    Taylor, S.4    Cushman, S.5
  • 43
    • 0035786915 scopus 로고    scopus 로고
    • The adipocyte as a secretory organ: Mechanisms of vesicle transport and secretory pathways
    • Bradley R, Cleveland K, Cheatham B. The adipocyte as a secretory organ: mechanisms of vesicle transport and secretory pathways. Recent Prog Horm Res 2001; 53: 329-358.
    • (2001) Recent Prog. Horm. Res , vol.53 , pp. 329-358
    • Bradley, R.1    Cleveland, K.2    Cheatham, B.3
  • 44
    • 0033680070 scopus 로고    scopus 로고
    • Identification and characterization of leptin-containing intracellular compartment in rat adipose cells
    • Roh C, Thoidis G, Farmer S, Kandror K. Identification and characterization of leptin-containing intracellular compartment in rat adipose cells. Am J Physiol Endocrinol Metab 2000; 279: E893-E899.
    • (2000) Am. J. Physiol. Endocrinol. Metab , vol.279
    • Roh, C.1    Thoidis, G.2    Farmer, S.3    Kandror, K.4
  • 45
    • 0035929647 scopus 로고    scopus 로고
    • Lipoprotein lipase and leptin are accumulated in different secretory compartments in rat adipocytes
    • Roh C, Roduit R, Thorens B, Fried S, Kandror K. Lipoprotein lipase and leptin are accumulated in different secretory compartments in rat adipocytes. J Biol Chem 2001; 276: 35 990-35 994.
    • (2001) J. Biol. Chem , vol.276
    • Roh, C.1    Roduit, R.2    Thorens, B.3    Fried, S.4    Kandror, K.5
  • 47
    • 0005174953 scopus 로고    scopus 로고
    • The crystal structure of a complement 1q family protein suggests an evolutionary link to tumor necrosis factor
    • Shapiro L, Scherer P. The crystal structure of a complement 1q family protein suggests an evolutionary link to tumor necrosis factor. Curr Biol 1998; 276: 3628-3634.
    • (1998) Curr. Biol , vol.276 , pp. 3628-3634
    • Shapiro, L.1    Scherer, P.2
  • 48
    • 0036134187 scopus 로고    scopus 로고
    • Resistin and obesity-associated insulin resistance
    • Steppan C, Lazar M. Resistin and obesity-associated insulin resistance. Trends Endocrinol Metab 2002; 13: 18-23.
    • (2002) Trends. Endocrinol. Metab , vol.13 , pp. 18-23
    • Steppan, C.1    Lazar, M.2
  • 49
    • 4243645912 scopus 로고    scopus 로고
    • Induction of adipocyte complement-related protein of 30 kilodaltons by PPARgamma agonists: A potential mechanism of insulin sensitization
    • Combs T, Wagner J, Berger J, et al. Induction of adipocyte complement-related protein of 30 kilodaltons by PPARgamma agonists: a potential mechanism of insulin sensitization. Endocrinology 2002; 143: 998-1007.
    • (2002) Endocrinology , vol.143 , pp. 998-1007
    • Combs, T.1    Wagner, J.2    Berger, J.3
  • 50
    • 0033538869 scopus 로고    scopus 로고
    • Two compartments for insulin-stimulated exocytosis in 3T3L1 adipocytes defined by endogenous ACRP30 and GLUT4
    • Bogan JS, Lodish HF. Two compartments for insulin-stimulated exocytosis in 3T3L1 adipocytes defined by endogenous ACRP30 and GLUT4. J Cell Biol 1999; 146: 609-620.
    • (1999) J. Cell. Biol , vol.146 , pp. 609-620
    • Bogan, J.S.1    Lodish, H.F.2
  • 52
    • 0026661997 scopus 로고
    • Effects of insulin on steady state kinetics of GLUT4 subcellular distribution in rat adipocytes
    • Jhun BH, Rampal AL, Liu H, Lachaal M, Jung CY. Effects of insulin on steady state kinetics of GLUT4 subcellular distribution in rat adipocytes. J Biol Chem 1992; 267: 17 710-17 715.
    • (1992) J. Biol. Chem , vol.267
    • Jhun, B.H.1    Rampal, A.L.2    Liu, H.3    Lachaal, M.4    Jung, C.Y.5
  • 53
    • 0026782176 scopus 로고
    • Immunocytochemical and biochemical studies of GLUT4 in rat skeletal muscle
    • Rodnick KJ, Slot JW, Studelska DR, et al. Immunocytochemical and biochemical studies of GLUT4 in rat skeletal muscle. J Biol Chem 1992; 267: 6278-6285.
    • (1992) J. Biol. Chem , vol.267 , pp. 6278-6285
    • Rodnick, K.J.1    Slot, J.W.2    Studelska, D.R.3
  • 54
    • 0027532611 scopus 로고
    • Comparison of GLUT4 and GLUT1 subcellular trafficking in basal and insulin-stimulated 3T3-L1 cells
    • Yang J, Holman GD. 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
  • 55
    • 0024370684 scopus 로고
    • Insulin-regulated glucose uptake in rat adipocytes is mediated by two transporter isoforms present in at least two vesicle populations
    • Zorzano A, Wilkinson W, Kotliar N, et al. Insulin-regulated glucose uptake in rat adipocytes is mediated by two transporter isoforms present in at least two vesicle populations. J Biol Chem 1989; 264: 12 358-12 363.
    • (1989) J. Biol. Chem , vol.264
    • Zorzano, A.1    Wilkinson, W.2    Kotliar, N.3
  • 56
    • 0030873897 scopus 로고    scopus 로고
    • Identification and characterization of two distinct intracellular GLUT4 pools in rat skeletal muscle: Evidence for an endosomal and an insulin-sensitive GLUT4 compartment
    • Aledo JC, Lavoie L, Volchuk A, Keller SR, Klip A, Hundal HS. Identification and characterization of two distinct intracellular GLUT4 pools in rat skeletal muscle: evidence for an endosomal and an insulin-sensitive GLUT4 compartment. Biochem J 1997; 325: 727-732.
    • (1997) Biochem. J , vol.325 , pp. 727-732
    • Aledo, J.C.1    Lavoie, L.2    Volchuk, A.3    Keller, S.R.4    Klip, A.5    Hundal, H.S.6
  • 57
    • 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, Lyttle C, 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.2    Lyttle, C.3
  • 58
    • 0032719409 scopus 로고    scopus 로고
    • Differential regulation of secretory compartments containing the insulin-responsive glucose transporter 4 in 3T3-L1 adipocytes
    • Millar C, Shewan A, Hickson G, James D, Gould G. 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.1    Shewan, A.2    Hickson, G.3    James, D.4    Gould, G.5
  • 59
    • 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 KS, Itakura H, Lane MD, 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 USA 1995; 92: 865-869.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 865-869
    • Ikemoto, S.1    Thompson, K.S.2    Itakura, H.3    Lane, M.D.4    Ezaki, O.5
  • 60
    • 0028287972 scopus 로고
    • Exercise induces rapid increases in GLUT4 expression, glucose transport capacity, and insulin-stimulated glycogen storage in muscle
    • Ren JM, Semenkovich CF, Gulve EA, Gao J, Holloszy JO. Exercise induces rapid increases in GLUT4 expression, glucose transport capacity, and insulin-stimulated glycogen storage in muscle. J Biol Chem 1994; 269: 14 396-14 401.
    • (1994) J. Biol. Chem , vol.269
    • Ren, J.M.1    Semenkovich, C.F.2    Gulve, E.A.3    Gao, J.4    Holloszy, J.O.5
  • 61
    • 0030808673 scopus 로고    scopus 로고
    • Osmotic shock stimulates GLUT4 translocation in 3T3L1 adipocytes by a novel tyrosine kinase pathway
    • Chen D, Elmendorf JS, Olson AL, Li X, Earp HS, Pessin JE. Osmotic shock stimulates GLUT4 translocation in 3T3L1 adipocytes by a novel tyrosine kinase pathway. J Biol Chem 1997; 272: 27 401-27 410.
    • (1997) J. Biol. Chem , vol.272
    • Chen, D.1    Elmendorf, J.S.2    Olson, A.L.3    Li, X.4    Earp, H.S.5    Pessin, J.E.6
  • 62
    • 0032557441 scopus 로고    scopus 로고
    • Guanosine 5′-O-(3-thiotriphosphate) (GTPgammaS) stimulation of GLUT4 translocation is tyrosine kinase-dependent
    • Elmendorf JS, Chen D, Pessin JE. Guanosine 5′-O-(3-thiotriphosphate) (GTPgammaS) stimulation of GLUT4 translocation is tyrosine kinase-dependent. J Biol Chem 1998; 273: 13289-13296.
    • (1998) J. Biol. Chem , vol.273 , pp. 13289-13296
    • Elmendorf, J.S.1    Chen, D.2    Pessin, J.E.3
  • 63
    • 0023951197 scopus 로고
    • Ligand-dependent intersubunit association within the insulin receptor complex activates its intrinsic kinase activity
    • Boni-Schnetzler M, Kaligian A, DelVecchio R, Pilch PF. Ligand-dependent intersubunit association within the insulin receptor complex activates its intrinsic kinase activity. J Biol Chem 1988; 263: 6822-6828.
    • (1988) J. Biol. Chem , vol.263 , pp. 6822-6828
    • Boni-Schnetzler, M.1    Kaligian, A.2    DelVecchio, R.3    Pilch, P.F.4
  • 64
    • 0024450708 scopus 로고
    • Autophosphorylation activates the soluble cytoplasmic domain of the insulin receptor in an intermolecular reaction
    • Cobb MH, Sand B-C, Gonzalez R, Goldsmith E, Ellis L. Autophosphorylation activates the soluble cytoplasmic domain of the insulin receptor in an intermolecular reaction. J Biol Chem 1989; 264: 18 701-18 706.
    • (1989) J. Biol. Chem , vol.264
    • Cobb, M.H.1    Sand, B.-C.2    Gonzalez, R.3    Goldsmith, E.4    Ellis, L.5
  • 65
    • 0026592871 scopus 로고
    • The reversible and irreversible autophosphorylations of insulin receptor kinase
    • Argetsinger LS, Shafer JA. The reversible and irreversible autophosphorylations of insulin receptor kinase. J Biol Chem 1992; 267: 22 095-22 101.
    • (1992) J. Biol. Chem , vol.267
    • Argetsinger, L.S.1    Shafer, J.A.2
  • 66
    • 0024456657 scopus 로고
    • Intermolecular transphosphorylation between insulin receptors and EGF-insulin receptor chimerae
    • Ballotti R, Lammers R, Scimeca J-C, et al. Intermolecular transphosphorylation between insulin receptors and EGF-insulin receptor chimerae. EMBO J 1989; 8: 3303-3309.
    • (1989) EMBO J , vol.8 , pp. 3303-3309
    • Ballotti, R.1    Lammers, R.2    Scimeca, J.-C.3
  • 67
    • 0030780254 scopus 로고    scopus 로고
    • The IRS-signaling system: A network of docking proteins that mediate insulin and cytokine action
    • White MF, Yenush L. The IRS-signaling system: a network of docking proteins that mediate insulin and cytokine action. Curr Top Microbiol Immunol 1998; 228: 179-208.
    • (1998) Curr. Top. Microbiol. Immunol , vol.228 , pp. 179-208
    • White, M.F.1    Yenush, L.2
  • 68
    • 0027212268 scopus 로고
    • The new elements of insulin signaling. Insulin receptor substrate-1 and proteins with SH2 domains
    • Myers M, White M. The new elements of insulin signaling. Insulin receptor substrate-1 and proteins with SH2 domains. Diabetes 1993; 42: 643-650.
    • (1993) Diabetes , vol.42 , pp. 643-650
    • Myers, M.1    White, M.2
  • 69
    • 0028242350 scopus 로고
    • Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor
    • Sasaoka T, Rose D, Jhun B, Saltiel A, Draznin B, Olefsky J. Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor. J Biol Chem 1994; 269: 13 689-13 694.
    • (1994) J. Biol. Chem , vol.269
    • Sasaoka, T.1    Rose, D.2    Jhun, B.3    Saltiel, A.4    Draznin, B.5    Olefsky, J.6
  • 70
    • 0028352043 scopus 로고
    • Role of IRS-1-Shc complexes in insulin signaling
    • Myers MGJ, Wanf L-M, Sun XJ, et al. Role of IRS-1-Shc complexes in insulin signaling. Mol Cell Biol 1994; 14: 3577-3587.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 3577-3587
    • Myers, M.G.J.1    Wanf, L.-M.2    Sun, X.J.3
  • 71
    • 0033574585 scopus 로고    scopus 로고
    • Identification of the APS protein as a nobel insulin receptor substrate
    • Moodie S, Alleman-Sposeto J, Gustafson T. Identification of the APS protein as a nobel insulin receptor substrate. J Biol Chem 1999; 274: 11 186-11 193.
    • (1999) J. Biol. Chem , vol.274
    • Moodie, S.1    Alleman-Sposeto, J.2    Gustafson, T.3
  • 72
    • 0030837119 scopus 로고    scopus 로고
    • Insulin stimulates tyrosine phosphorylation of the proto-oncogene product of c-Cbl in 3T3-L1 adipocytes
    • Ribon V, Saltiel AR. Insulin stimulates tyrosine phosphorylation of the proto-oncogene product of c-Cbl in 3T3-L1 adipocytes. Biochem J 1997; 324: 839-845.
    • (1997) Biochem. J , vol.324 , pp. 839-845
    • Ribon, V.1    Saltiel, A.R.2
  • 73
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh W, Williams L. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 1994; 266: 1862-1865.
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.1    Williams, L.2
  • 74
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh WM, Turck CW, Williams LT. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 1995; 268: 1177-1179.
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 75
    • 0028888604 scopus 로고
    • The PTB domain: A new protein module implicated in signal transduction
    • Van der Geer P, Pawson T. The PTB domain: a new protein module implicated in signal transduction. Trends Biochem Sci 1995; 20: 277-280.
    • (1995) Trends. Biochem. Sci , vol.20 , pp. 277-280
    • Van der Geer, P.1    Pawson, T.2
  • 76
    • 0029640799 scopus 로고
    • A phosphotyrosine interaction domain
    • Bork P, Margolis B. A phosphotyrosine interaction domain. Cell 1995; 80: 693, 694.
    • (1995) Cell , vol.80 , pp. 693-694
    • Bork, P.1    Margolis, B.2
  • 77
    • 0028874953 scopus 로고
    • PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities
    • Wolf G, Trub T, Ottinger E, et al. PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J Biol Chem 1995; 270: 27 407-27 410.
    • (1995) J. Biol. Chem , vol.270
    • Wolf, G.1    Trub, T.2    Ottinger, E.3
  • 78
    • 0030010590 scopus 로고    scopus 로고
    • Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor
    • Eck MJ, Dhe-Paganon S, Trub T, Nolte RT, Shoelson SE. Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor. Cell 1996; 85: 695-705.
    • (1996) Cell , vol.85 , pp. 695-705
    • Eck, M.J.1    Dhe-Paganon, S.2    Trub, T.3    Nolte, R.T.4    Shoelson, S.E.5
  • 79
    • 0026660653 scopus 로고
    • Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation
    • Backer JM, Myers Jr MG, Shoelson SE, et al. Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J 1992; 11: 3469-3479.
    • (1992) EMBO J , vol.11 , pp. 3469-3479
    • Backer, J.M.1    Myers M.G., Jr.2    Shoelson, S.E.3
  • 80
    • 0027416751 scopus 로고
    • Association of IRS-1 with the insulin receptor and the phosphatidylinositol 3′-kinase
    • Backer JM, Myers MGJ, Sun X-J, et al. Association of IRS-1 with the insulin receptor and the phosphatidylinositol 3′-kinase. J Biol Chem 1993; 268(11): 8204-8212.
    • (1993) J. Biol. Chem , vol.268 , Issue.11 , pp. 8204-8212
    • Backer, J.M.1    Myers, M.G.J.2    Sun, X.-J.3
  • 81
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B, Aless ID. The PI3K-PDK1 connection: more than just a road to PKB. Biochem J 2000; 346: 561-576.
    • (2000) Biochem. J , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Aless, I.D.2
  • 82
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering BM, Coffer PJ. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 1995; 376: 599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 83
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the AKT-1 protein-kinase to phosphatidylinositol-3,4,5-trisphosphate without subsequent activation
    • James SR, Downes CP, Gigg R, Grove SJA, Holmes AB, Alessi DR. Specific binding of the AKT-1 protein-kinase to phosphatidylinositol-3,4,5-trisphosphate without subsequent activation. Biochem J 1996; 315: 709-713.
    • (1996) Biochem. J , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.A.4    Holmes, A.B.5    Alessi, D.R.6
  • 84
    • 0031015986 scopus 로고    scopus 로고
    • A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
    • Klippel A, Kavanaugh WM, Pot D, Williams LT. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol Cell Biol 1997; 17: 338-344.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 338-344
    • Klippel, A.1    Kavanaugh, W.M.2    Pot, D.3    Williams, L.T.4
  • 85
    • 0028560447 scopus 로고
    • Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P-2 and PtdIns-3,4,5-P-3
    • Toker A, Meyer M, Reddy KK, et al. Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P-2 and PtdIns-3,4,5-P-3. J Biol Chem 1994; 269: 32 358-32 367.
    • (1994) J. Biol. Chem , vol.269
    • Toker, A.1    Meyer, M.2    Reddy, K.K.3
  • 86
    • 0031724590 scopus 로고    scopus 로고
    • Requirement of atypical protein kinase Clambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes
    • Kotani K, Ogawa W, Matsumoto M, et al. Requirement of atypical protein kinase Clambda 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
  • 87
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good JA, Ziegler WH, Parekh DB, Alessi DR, Cohen P, Parker PJ. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 1998; 281: 2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 88
    • 0035830320 scopus 로고    scopus 로고
    • Insulin and PIP3 activate PKC-zeta by mechanisms that are both dependent and independent of phosphorylation of activation loop (T410) and autophosphorylation (T560) sites
    • Standaert M, Bandyopadhyay G, Kanoh Y, Sajan M, Farese R. Insulin and PIP3 activate PKC-zeta by mechanisms that are both dependent and independent of phosphorylation of activation loop (T410) and autophosphorylation (T560) sites. Biochemistry 2001; 40: 249-255.
    • (2001) Biochemistry , vol.40 , pp. 249-255
    • Standaert, M.1    Bandyopadhyay, G.2    Kanoh, Y.3    Sajan, M.4    Farese, R.5
  • 89
    • 0030734345 scopus 로고    scopus 로고
    • Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells
    • Cong LN, Chen H, Li Y, et al. Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. Mol Endocrinol 1997; 11: 1881-1890.
    • (1997) Mol. Endocrinol , vol.11 , pp. 1881-1890
    • Cong, L.N.1    Chen, H.2    Li, Y.3
  • 90
    • 0031841949 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide
    • Summers SA, Garza LA, Zhou H, Birnbaum MJ. Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide. Mol Cell Biol 1998; 18: 5457-5464.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 5457-5464
    • Summers, S.A.1    Garza, L.A.2    Zhou, H.3    Birnbaum, M.J.4
  • 91
    • 0033049422 scopus 로고    scopus 로고
    • Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts
    • Wang Q, Somwar R, Bilan PJ, et al. Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts. Mol Cell Biol 1999; 19: 4008-4018.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4008-4018
    • Wang, Q.1    Somwar, R.2    Bilan, P.J.3
  • 92
    • 0344614675 scopus 로고    scopus 로고
    • Potential role of 3-phosphoinositide-dependent protein kinase 1 (PDK1) in insulin-stimulated glucose transporter 4 translocation in adipocytes
    • Grillo S, Gremeaux T, Le Marchand-Brustel Y, Tanti J. Potential role of 3-phosphoinositide-dependent protein kinase 1 (PDK1) in insulin-stimulated glucose transporter 4 translocation in adipocytes. FEBS Lett 1999; 461: 277-279.
    • (1999) FEBS Lett , vol.461 , pp. 277-279
    • Grillo, S.1    Gremeaux, T.2    Le Marchand-Brustel, Y.3    Tanti, J.4
  • 93
    • 0033604612 scopus 로고    scopus 로고
    • Insulin signaling regulating the trafficking and plasma membrane fusion of GLUT4-containing intracellular vesicles
    • Elmendorf J, Pessin J. Insulin signaling regulating the trafficking and plasma membrane fusion of GLUT4-containing intracellular vesicles. Exp Cell Res 1999; 253: 55-62.
    • (1999) Exp. Cell. Res , vol.253 , pp. 55-62
    • Elmendorf, J.1    Pessin, J.2
  • 94
    • 0028132214 scopus 로고
    • Insulin receptor substrate 1 mediates the stimulatory effect of insulin on GLUT4 translocation in transfected rat adipose cells
    • Quon MJ, Butte AJ, Zarnowski MJ, Sesti G, Cushman SW, Taylor SI. Insulin receptor substrate 1 mediates the stimulatory effect of insulin on GLUT4 translocation in transfected rat adipose cells. J Biol Chem 1994; 269(45): 27 920-27 924.
    • (1994) J. Biol. Chem , vol.269 , Issue.45
    • Quon, M.J.1    Butte, A.J.2    Zarnowski, M.J.3    Sesti, G.4    Cushman, S.W.5    Taylor, S.I.6
  • 95
    • 0028308412 scopus 로고
    • Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation
    • Cheatham B, Vlahos CJ, Cheatham L, Wang L, Blenis J, Kahn CR. Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation. Mol Cell Biol 1994; 14: 4902-4911.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 4902-4911
    • Cheatham, B.1    Vlahos, C.J.2    Cheatham, L.3    Wang, L.4    Blenis, J.5    Kahn, C.R.6
  • 96
    • 0028124189 scopus 로고
    • Essential role of phophatidylinositol 3-kinase in insulin-induced glucose transport and antilypolysis in rat adipocytes. Studies with a selective inhibitor wortmannin
    • Okada T, Kawano Y, Sakakibara R, Hazeki O, Ui M. Essential role of phophatidylinositol 3-kinase in insulin-induced glucose transport and antilypolysis in rat adipocytes. Studies with a selective inhibitor wortmannin. J Biol Chem 1994; 269: 3568-3573.
    • (1994) J. Biol. Chem , vol.269 , pp. 3568-3573
    • Okada, T.1    Kawano, Y.2    Sakakibara, R.3    Hazeki, O.4    Ui, M.5
  • 97
    • 0031806103 scopus 로고    scopus 로고
    • Requirement for activation of the serine-threonine kinase Akt (protein kinase B) in insulin stimulation of protein synthesis but not of glucose transport
    • Kitamura T, Ogawa W, Sakaue H, et al. Requirement for activation of the serine-threonine kinase Akt (protein kinase B) in insulin stimulation of protein synthesis but not of glucose transport. Mol Cell Biol 1998; 18: 3708-3717.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 3708-3717
    • Kitamura, T.1    Ogawa, W.2    Sakaue, H.3
  • 98
    • 0035135318 scopus 로고    scopus 로고
    • Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 5′-phosphatase catalytic activity
    • Wada T, Sasaoka T, Funaki M, et al. Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 5′-phosphatase catalytic activity. Mol Cell Biol 2001; 21: 1633-1646.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 1633-1646
    • Wada, T.1    Sasaoka, T.2    Funaki, M.3
  • 99
    • 0025042770 scopus 로고
    • Phosphorylation of the PDGF receptor? subunit creates a tight binding site for phosphatidylinositol 3 kinase
    • Kazlauskas A, Cooper JA. Phosphorylation of the PDGF receptor? subunit creates a tight binding site for phosphatidylinositol 3 kinase. EMBO J 1990; 9: 3279-3286.
    • (1990) EMBO J , vol.9 , pp. 3279-3286
    • Kazlauskas, A.1    Cooper, J.A.2
  • 100
    • 0028865424 scopus 로고
    • The inability of phosphatidylinositol 3-kinase activation to stimulate GLUT4 translocation indicates additional signaling pathways are required for insulin-stimulated glucose uptake
    • Isakoff SJ, Taha C, Rose E, Marcusohn J, Klip A, Skolnik EY. The inability of phosphatidylinositol 3-kinase activation to stimulate GLUT4 translocation indicates additional signaling pathways are required for insulin-stimulated glucose uptake. Proc Natl Acad Sci USA 1995; 92: 10 247-10 251.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92
    • Isakoff, S.J.1    Taha, C.2    Rose, E.3    Marcusohn, J.4    Klip, A.5    Skolnik, E.Y.6
  • 101
    • 0032509202 scopus 로고    scopus 로고
    • Stimulation of IRS-1-associated phosphatidylinositol 3-kinase and Akt/protein kinase B but not glucose transport by beta1-integrin signaling in rat adipocytes
    • Guilherme A, Czech MP. Stimulation of IRS-1-associated phosphatidylinositol 3-kinase and Akt/protein kinase B but not glucose transport by beta1-integrin signaling in rat adipocytes. J Biol Chem 1998; 273: 33 119-33 122.
    • (1998) J. Biol. Chem , vol.273
    • Guilherme, A.1    Czech, M.P.2
  • 102
    • 14444276528 scopus 로고    scopus 로고
    • Two naturally occurring insulin receptor tyrosine kinase domain mutants provide evidence that phosphoinositide 3-kinase activation alone is not sufficient for the mediation of insulin's metabolic and mitogenic effects
    • Krook A, Whitehead J, Dobson S, et al. Two naturally occurring insulin receptor tyrosine kinase domain mutants provide evidence that phosphoinositide 3-kinase activation alone is not sufficient for the mediation of insulin's metabolic and mitogenic effects. J Biol Chem 1997; 272: 30 208-30 214.
    • (1997) J. Biol. Chem , vol.272
    • Krook, A.1    Whitehead, J.2    Dobson, S.3
  • 104
    • 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, Saltiel A. APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes. Mol Cell Biol 2002; 11: 3599-3609.
    • (2002) Mol. Cell. Biol , vol.11 , pp. 3599-3609
    • Liu, J.1    Kimura, A.2    Baumann, C.3    Saltiel, A.4
  • 105
    • 0031594145 scopus 로고    scopus 로고
    • A novel, multifunctional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes
    • Ribon V, Saltiel A. A novel, multifunctional 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    Saltiel, A.2
  • 106
    • 0035979221 scopus 로고    scopus 로고
    • The sorbin homology domain: A motif for the targeting of proteins to lipid rafts
    • Kimura A, Baumann C, Chiang S, Saltiel A. The sorbin homology domain: a motif for the targeting of proteins to lipid rafts. Proc Natl Acad Sci USA 2001; 98: 9098-9103.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9098-9103
    • Kimura, A.1    Baumann, C.2    Chiang, S.3    Saltiel, A.4
  • 107
    • 0034648794 scopus 로고    scopus 로고
    • CAP defines a second signalling pathway required for insulin-stimulated glucose transport
    • Baumann C, Ribon V, Kanzaki M, et al. CAP defines a second signalling pathway required for insulin-stimulated glucose transport. Nature 2000; 407: 202-207.
    • (2000) Nature , vol.407 , pp. 202-207
    • Baumann, C.1    Ribon, V.2    Kanzaki, M.3
  • 108
    • 0029655999 scopus 로고    scopus 로고
    • The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner
    • Ribon V, Hubbell S, Herrera R, Saltiel AR. The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner. Mol Cell Biol 1996; 16: 45-52.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 45-52
    • Ribon, V.1    Hubbell, S.2    Herrera, R.3    Saltiel, A.R.4
  • 109
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors-signalling complex formation and biological roles
    • Feller S. Crk family adaptors-signalling complex formation and biological roles. Oncogene 2001; 20: 6348-6371.
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.1
  • 110
    • 0035921433 scopus 로고    scopus 로고
    • Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation
    • Watson R, Shigematsu S, Chiang S, et al. Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation. J Biol Chem 2001; 154: 829-840.
    • (2001) J. Biol. Chem , vol.154 , pp. 829-840
    • Watson, R.1    Shigematsu, S.2    Chiang, S.3
  • 111
    • 0035834644 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling
    • Kanzaki M, Pessin JE. Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling. J Biol Chem 2001; 276: 42 436-42 444.
    • (2001) J. Biol. Chem , vol.276
    • Kanzaki, M.1    Pessin, J.E.2
  • 112
    • 0037066760 scopus 로고    scopus 로고
    • Cloning and functional characterization of related TC10 isoforms, a subfamily of Rho proteins involved in insulin-stimulated glucose transport
    • Chiang S, Hou J, Hwang J, Pessin J, Saltiel A. Cloning and functional characterization of related TC10 isoforms, a subfamily of Rho proteins involved in insulin-stimulated glucose transport. J Biol Chem 2002; 277: 13 067-13 073.
    • (2002) J. Biol. Chem , vol.277
    • Chiang, S.1    Hou, J.2    Hwang, J.3    Pessin, J.4    Saltiel, A.5
  • 113
    • 0023013903 scopus 로고
    • Insulin-like growth factors, insulin, and epidermal growth factor cause rapid cytoskeletal reorganization in KB cells. Clarification of the roles of type I insulin-like growth factor receptors and insulin receptors
    • Kadowaki T, Koyasu S, Nishida E, et al. Insulin-like growth factors, insulin, and epidermal growth factor cause rapid cytoskeletal reorganization in KB cells. Clarification of the roles of type I insulin-like growth factor receptors and insulin receptors. J Biol Chem 1986; 261: 16 141-16 147.
    • (1986) J. Biol. Chem , vol.261
    • Kadowaki, T.1    Koyasu, S.2    Nishida, E.3
  • 114
    • 0034724747 scopus 로고    scopus 로고
    • The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes
    • Nakashima N, Sharma P, Imamura T, Bookstein R, Olefsky J. The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes. J Biol Chem 2000; 275: 12 889-12 895.
    • (2000) J. Biol. Chem , vol.275
    • Nakashima, N.1    Sharma, P.2    Imamura, T.3    Bookstein, R.4    Olefsky, J.5
  • 115
    • 0029973135 scopus 로고    scopus 로고
    • Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes
    • Martin SS, Haruta T, Morris AJ, Klippel A, Williams LT, Olefsky JM. Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes. J Biol Chem 1996; 271: 17 605-17 608.
    • (1996) J. Biol. Chem , vol.271
    • Martin, S.S.1    Haruta, T.2    Morris, A.J.3    Klippel, A.4    Williams, L.T.5    Olefsky, J.M.6
  • 116
    • 0034907579 scopus 로고    scopus 로고
    • Insulin-induced cortical actin remodeling promotes GLUT4 insertion at muscle cell membrane ruffles
    • Tong P, Khayat Z, 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.2    Huang, C.3    Patel, N.4    Ueyama, A.5    Klip, A.6
  • 117
    • 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, et al. Insulin action on GLUT4 traffic visualized in single 3T3-l1 adipocytes by using ultra-fast microscopy. Mol Cell Biol 2001; 12: 129-141.
    • (2001) Mol. Cell. Biol , vol.12 , pp. 129-141
    • Patki, V.1    Buxton, J.2    Chawla, A.3
  • 118
    • 0034162776 scopus 로고    scopus 로고
    • Actin filaments play a critical role in insulin-induced exocytotic recruitment but not in endocytosis of GLUT4 in isolated rat adipocytes
    • Omata W, Shibata H, Li L, Takata K, Kojima I. Actin filaments play a critical role in insulin-induced exocytotic recruitment but not in endocytosis of GLUT4 in isolated rat adipocytes. Biochem J 2000; 346: 321-328.
    • (2000) Biochem. J , vol.346 , pp. 321-328
    • Omata, W.1    Shibata, H.2    Li, L.3    Takata, K.4    Kojima, I.5
  • 119
    • 0033166311 scopus 로고    scopus 로고
    • Cellular functions of TC10, a Rho family GTPase: Regulation of morphology, signal transduction and cell growth
    • Murphy G, Solski P, Jillian S, et al. Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth. Oncogene 1999; 18: 3831-3845.
    • (1999) Oncogene , vol.18 , pp. 3831-3845
    • Murphy, G.1    Solski, P.2    Jillian, S.3
  • 120
    • 0037016725 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase-independent insulin signaling pathway to N-WASP/Arp2/3/F-actin required for GLUT4 glucose transporter recycling
    • Jiang Z, Chawla A, Bose A, Way M, Czech M. A phosphatidylinositol 3-kinase-independent insulin signaling pathway to N-WASP/Arp2/3/F-actin required for GLUT4 glucose transporter recycling. J Biol Chem 2002; 277: 509-515.
    • (2002) J. Biol. Chem , vol.277 , pp. 509-515
    • Jiang, Z.1    Chawla, A.2    Bose, A.3    Way, M.4    Czech, M.5
  • 121
    • 0032911883 scopus 로고    scopus 로고
    • An SH2 domain-containing 5′ inositolphosphatase inhibits insulin-induced GLUT4 translocation and growth factor-induced actin filament rearrangement
    • Vollenweider P, Clodi M, Martin S, Imamura T, Kavanaugh W, Olefsky J. An SH2 domain-containing 5′ inositolphosphatase inhibits insulin-induced GLUT4 translocation and growth factor-induced actin filament rearrangement. Mol Cell Biol 1999; 19: 1081-1091.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 1081-1091
    • Vollenweider, P.1    Clodi, M.2    Martin, S.3    Imamura, T.4    Kavanaugh, W.5    Olefsky, J.6
  • 122
    • 0034624990 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton
    • Dong L, Landa L, Wick M, et al. Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton. Proc Natl Acad Sci USA 2000; 97: 5089-5094.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5089-5094
    • Dong, L.1    Landa, L.2    Wick, M.3
  • 123
    • 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, Welsh G, Oatey P, Tavare J. Role for the microtubule cytoskeleton in GLUT4 vesicle trafficking and in the regulation of insulin-stimulated glucose uptake. Biochem J 2000; 352: 267-276.
    • (2000) Biochem. J , vol.352 , pp. 267-276
    • Fletcher, L.1    Welsh, G.2    Oatey, P.3    Tavare, J.4
  • 124
    • 0034624008 scopus 로고    scopus 로고
    • Perinuclear localization and insulin-responsiveness of GLUT4 requires cytoskeletal integrity in 3T3-L1 adipocytes
    • Guilherme A, Emoto M, Buxton J, et al. Perinuclear localization and insulin-responsiveness of GLUT4 requires cytoskeletal integrity in 3T3-L1 adipocytes. J Biol Chem 2000; 275: 38 151-38 159.
    • (2000) J. Biol. Chem , vol.275
    • Guilherme, A.1    Emoto, M.2    Buxton, J.3
  • 125
    • 0035815634 scopus 로고    scopus 로고
    • Insulin-mediated GLUT4 translocation is dependent on the microtubule network
    • Olson A, Trumbly A, Gibson G. Insulin-mediated GLUT4 translocation is dependent on the microtubule network. J Biol Chem 2001; 276: 10 706-10 714.
    • (2001) J. Biol. Chem , vol.276
    • Olson, A.1    Trumbly, A.2    Gibson, G.3
  • 126
    • 0035815710 scopus 로고    scopus 로고
    • A role for kinesin in insulin-stimulated GLUT4 glucose transporter translocation in 3t3-L1 adipocytes
    • Emoto M, Langille S, Czech M. A role for kinesin in insulin-stimulated GLUT4 glucose transporter translocation in 3t3-L1 adipocytes. J Biol Chem 2001; 276: 10 677-10 682.
    • (2001) J. Biol. Chem , vol.276
    • Emoto, M.1    Langille, S.2    Czech, M.3
  • 127
    • 0032504208 scopus 로고    scopus 로고
    • Endocytosis of the glucose transporter GLUT4 is mediated by the GTPase dynamin
    • Al-Hasani H, Hinck CS, Cushman SW. Endocytosis of the glucose transporter GLUT4 is mediated by the GTPase dynamin. J Biol Chem 1998; 273: 17 504-17 510.
    • (1998) J. Biol. Chem , vol.273
    • Al-Hasani, H.1    Hinck, C.S.2    Cushman, S.W.3
  • 128
    • 0034041405 scopus 로고    scopus 로고
    • Functional comparison of the role of dynamin 2 splice variants on GLUT-4 endocytosis in 3T3L1 adipocytes
    • Kao A, Yang C, Pessin J. Functional comparison of the role of dynamin 2 splice variants on GLUT-4 endocytosis in 3T3L1 adipocytes. Am J Physiol Endocrinol Metab 2000; 278: E825-E831.
    • (2000) Am. J. Physiol. Endocrinol. Metab , vol.278
    • Kao, A.1    Yang, C.2    Pessin, J.3
  • 129
    • 0032478621 scopus 로고    scopus 로고
    • Perturbation of dynamin II with an amphiphysin SH3 domain increases GLUT4 glucose transporters at the plasma membrane in 3T3-L1 adipocytes. Dynamin II participates in GLUT4 endocytosis
    • Volchuk A, Narine S, Foster LJ, Grabs D, De Camilli P, Klip A. Perturbation of dynamin II with an amphiphysin SH3 domain increases GLUT4 glucose transporters at the plasma membrane in 3T3-L1 adipocytes. Dynamin II participates in GLUT4 endocytosis. J Biol Chem 1998; 273: 8169-8176.
    • (1998) J. Biol. Chem , vol.273 , pp. 8169-8176
    • Volchuk, A.1    Narine, S.2    Foster, L.J.3    Grabs, D.4    De Camilli, P.5    Klip, A.6
  • 130
    • 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. Insulin can regulate GLUT4 internalization by signaling to Rab5 and the motor protein dynein. Proc Natl Acad Sci USA 2001; 98: 13 084-13 089.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98
    • Huang, J.1    Imamura, T.2    Olefsky, J.3
  • 131
    • 0028350057 scopus 로고
    • Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
    • Calakos N, Bennett MK, Peterson KE. Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science 1994; 263: 1146-1149.
    • (1994) Science , vol.263 , pp. 1146-1149
    • Calakos, N.1    Bennett, M.K.2    Peterson, K.E.3
  • 132
    • 0028491306 scopus 로고
    • Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release
    • Schiavo G, Rossetto O, Montecucco C. Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release. Semin Cell Biol 1994; 5: 221-229.
    • (1994) Semin. Cell. Biol , vol.5 , pp. 221-229
    • Schiavo, G.1    Rossetto, O.2    Montecucco, C.3
  • 133
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco C, Schiavo G. Mechanism of action of tetanus and botulinum neurotoxins. Mol Microbiol 1994; 13: 1-8.
    • (1994) Mol. Microbiol , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 134
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber T, Zemelman BV, McNew JA, et al. SNAREpins: minimal machinery for membrane fusion. Cell 1998; 92: 759-772.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3
  • 135
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson PI, Roth R, Morisaki H, Jahn R, Heuser JE. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 1997; 90: 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 136
    • 0032476605 scopus 로고    scopus 로고
    • Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex
    • Katz L, Hanson PI, Heuser JE, Brennwald P. Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex. EMBO J 1998; 17: 6200-6209.
    • (1998) EMBO J , vol.17 , pp. 6200-6209
    • Katz, L.1    Hanson, P.I.2    Heuser, J.E.3    Brennwald, P.4
  • 137
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. 4 A resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. 4 A resolution. Nature 1998; 395: 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 138
    • 0035798174 scopus 로고    scopus 로고
    • Cell biology. Fusion without SNAREs?
    • 1015
    • Scales S, Finley M, Scheller R. Cell biology. Fusion without SNAREs? Science 2001; 294: 1015, 1016.
    • (2001) Science , vol.294 , pp. 1016
    • Scales, S.1    Finley, M.2    Scheller, R.3
  • 139
    • 0033179852 scopus 로고    scopus 로고
    • Intracellular membrane fusion: SNAREs only?
    • Mayer A. Intracellular membrane fusion: SNAREs only? Curr Opin Cell Biol. 1999; 11: 447-452.
    • (1999) Curr. Opin. Cell. Biol , vol.11 , pp. 447-452
    • Mayer, A.1
  • 140
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer S. Transport-vesicle targeting: tethers before SNAREs. Nat Cell Biol. 1999; 1: E17-E22.
    • (1999) Nat. Cell. Biol , vol.1
    • Pfeffer, S.1
  • 141
    • 0030055490 scopus 로고    scopus 로고
    • Syntaxin 4 in 3T3-L1 adipocytes: Regulation by insulin and participation in insulin-dependent glucose transport
    • Volchuk A, Wang Q, Ewart HS, et al. Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport. Mol Biol Cell 1996; 7: 1075-1082.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1075-1082
    • Volchuk, A.1    Wang, Q.2    Ewart, H.S.3
  • 142
    • 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 AL, Knight JB, Pessin JE. 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
  • 143
    • 0030669618 scopus 로고    scopus 로고
    • Moving GLUT4: The biogenesis and trafficking of GLUT4 storage vesicles
    • Rea S, James DE. 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
  • 144
    • 0034677749 scopus 로고    scopus 로고
    • Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2
    • Kawanishi M, Tamori Y, Okazawa H, Araki S, Shinoda H, Kasuga M. Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2. J Biol Chem 2000; 275: 8240-8247.
    • (2000) J. Biol. Chem , vol.275 , pp. 8240-8247
    • Kawanishi, M.1    Tamori, Y.2    Okazawa, H.3    Araki, S.4    Shinoda, H.5    Kasuga, M.6
  • 145
    • 0035000661 scopus 로고    scopus 로고
    • Syntaxin 4 heterozygous knockout mice develop muscle insulin resistance
    • Yang C, Coker K, Kim J, et al. Syntaxin 4 heterozygous knockout mice develop muscle insulin resistance. J Clin Invest 2001; 107: 1311-1318.
    • (2001) J. Clin. Invest , vol.107 , pp. 1311-1318
    • Yang, C.1    Coker, K.2    Kim, J.3
  • 147
    • 17144463802 scopus 로고    scopus 로고
    • Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c
    • Araki S, Tamori Y, Kawanishi M, et al. Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c. Biochem Biophys Res Comm 1997; 234: 257-262.
    • (1997) Biochem. Biophys. Res. Comm , vol.234 , pp. 257-262
    • Araki, S.1    Tamori, Y.2    Kawanishi, M.3
  • 149
    • 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, et al. inhibition of insulin-induced GLUT4 translocation by Munc18c through interaction with syntaxin4 in 3T3-L1 adipocytes. J Biol Chem 1998; 273: 19 740-19 746.
    • (1998) J. Biol. Chem , vol.273
    • Tamori, Y.1    Kawanishi, M.2    Niki, T.3
  • 150
    • 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, Bilan P, Khayat Z, 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: 2403-2407.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2403-2407
    • Randhawa, V.1    Bilan, P.2    Khayat, Z.3
  • 151
    • 0033153025 scopus 로고    scopus 로고
    • Synip: A novel insulin-regulated syntaxin 4 binding protein mediating GLUT4 translocation in adipocytes
    • Min J, Okada S, Coker K, 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    Coker, K.3
  • 152
  • 153
    • 0035895983 scopus 로고    scopus 로고
    • Direct interaction of Rab4 with syntaxin 4
    • Li L, Omata W, Kojima I, Shibata H. Direct interaction of Rab4 with syntaxin 4. J Biol Chem 2001; 276: 5265-5273.
    • (2001) J. Biol. Chem , vol.276 , pp. 5265-5273
    • Li, L.1    Omata, W.2    Kojima, I.3    Shibata, H.4
  • 154
    • 0029887964 scopus 로고    scopus 로고
    • Compartment ablation analysis of the insulin-responsive glucose transporter (GLUT4) in 3T3-L1 adipocytes
    • Livingstone C, James D, Rice J, Hanpeter D, Gould G. 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.2    Rice, J.3    Hanpeter, D.4    Gould, G.5
  • 155
    • 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, Shewan A, Millar C, Gould G, James D. 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.1    Shewan, A.2    Millar, C.3    Gould, G.4    James, D.5
  • 156
    • 0035134281 scopus 로고    scopus 로고
    • VAMP3 null mice display normal constitutive, insulin- and exercise-regulated vesicle trafficking
    • Yang C, Mora S, Ryder J, et al. VAMP3 null mice display normal constitutive, insulin- and exercise-regulated vesicle trafficking. Mol Biol Cell 2001; 21: 1573-1580.
    • (2001) Mol. Biol. Cell , vol.21 , pp. 1573-1580
    • Yang, C.1    Mora, S.2    Ryder, J.3
  • 157
    • 0034679831 scopus 로고    scopus 로고
    • Discrimination of GLUT4 vesicle trafficking from fusion using a temperature-sensitive Munc18c mutant
    • Thurmond D, Pessin J. Discrimination of GLUT4 vesicle trafficking from fusion using a temperature-sensitive Munc18c mutant. EMBO J 2000; 19: 3565-3575.
    • (2000) EMBO J , vol.19 , pp. 3565-3575
    • Thurmond, D.1    Pessin, J.2
  • 158
    • 0033988446 scopus 로고    scopus 로고
    • Munc18c function is required for insulin-stimulated plasma membrane fusion of GLUT4 and insulin-responsive amino peptidase storage vesicles
    • Thurmond D, Kanzaki M, Khan A, Pessin J. Munc18c function is required for insulin-stimulated plasma membrane fusion of GLUT4 and insulin-responsive amino peptidase storage vesicles. Mol Cell Biol 2000; 20: 379-388.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 379-388
    • Thurmond, D.1    Kanzaki, M.2    Khan, A.3    Pessin, J.4
  • 159
    • 0036137684 scopus 로고    scopus 로고
    • Rab GTPases, intracellular traffic and disease
    • Seabra M, Mules E, Hume A. Rab GTPases, intracellular traffic and disease. Trends Mol Med 2002; 8: 23-30.
    • (2002) Trends. Mol. Med , vol.8 , pp. 23-30
    • Seabra, M.1    Mules, E.2    Hume, A.3
  • 160
    • 0036196195 scopus 로고    scopus 로고
    • Intracellular transport mechanisms of signal transducers
    • Dorn G, Mochly-Rosen D. Intracellular transport mechanisms of signal transducers. Annu Rev Physiol 2002; 64: 407-429.
    • (2002) Annu. Rev. Physiol , vol.64 , pp. 407-429
    • Dorn, G.1    Mochly-Rosen, D.2
  • 161
    • 0036468368 scopus 로고    scopus 로고
    • Rabs grab motors: Defining the connections between rab GTPases and motor proteins
    • Hammer J, Wu X. Rabs grab motors: defining the connections between rab GTPases and motor proteins. Curr Opin Cell Biol 2002; 14: 69-75.
    • (2002) Curr. Opin. Cell. Biol , vol.14 , pp. 69-75
    • Hammer, J.1    Wu, X.2
  • 162
    • 0036059819 scopus 로고    scopus 로고
    • Mosaic organization of the endocytic pathway
    • Miaczynska M, Zerial M. Mosaic organization of the endocytic pathway. Exp Cell Res 2002; 272: 8-14.
    • (2002) Exp. Cell. Res , vol.272 , pp. 8-14
    • Miaczynska, M.1    Zerial, M.2
  • 164
    • 0029984532 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the Rab4 hypervariable carboxyl-terminal domain inhibits insulin action on glucose transport in rat adipocytes
    • Shibata H, Omata W, Suzuki Y, Tanaka S, Kojima I. A synthetic peptide corresponding to the Rab4 hypervariable carboxyl-terminal domain inhibits insulin action on glucose transport in rat adipocytes. J Biol Chem 1996; 271: 9704-9709.
    • (1996) J. Biol. Chem , vol.271 , pp. 9704-9709
    • Shibata, H.1    Omata, W.2    Suzuki, Y.3    Tanaka, S.4    Kojima, I.5
  • 165
    • 0031007132 scopus 로고    scopus 로고
    • Association of cytosolic Rab4 with GDI isoforms in insulin-sensitive 3T3-L1 adipocytes
    • Shisheva A, Czech M. Association of cytosolic Rab4 with GDI isoforms in insulin-sensitive 3T3-L1 adipocytes. Biochemistry 1997; 36: 6564-6570.
    • (1997) Biochemistry , vol.36 , pp. 6564-6570
    • Shisheva, A.1    Czech, M.2
  • 166
    • 0030958276 scopus 로고    scopus 로고
    • Heterologous expression of rab4 reduces glucose transport and GLUT4 abundance at the cell surface in oocytes
    • Mora S, Monden I, Zorzano A, Keller K. Heterologous expression of rab4 reduces glucose transport and GLUT4 abundance at the cell surface in oocytes. Biochem J 1997; 324: 455-459.
    • (1997) Biochem. J , vol.324 , pp. 455-459
    • Mora, S.1    Monden, I.2    Zorzano, A.3    Keller, K.4
  • 167
    • 0034463845 scopus 로고    scopus 로고
    • Expression of a prenylation-deficient rab4 interferes with propagation of insulin signaling through insulin receptor substrate-1
    • Knight J, Cao K, Gibson G, Olson A. Expression of a prenylation-deficient rab4 interferes with propagation of insulin signaling through insulin receptor substrate-1. Endocrinology 2001; 141: 208-218.
    • (2001) Endocrinology , vol.141 , pp. 208-218
    • Knight, J.1    Cao, K.2    Gibson, G.3    Olson, A.4
  • 168
    • 0028951905 scopus 로고
    • Overexpression of wild-type and mutant ARF1 and ARF6: Distinct perturbations of nonoverlapping membrane compartments
    • Peters P, Hsu V, Ooi C, et al. Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J Biol Chem 1995; 128: 1003-1017.
    • (1995) J. Biol. Chem , vol.128 , pp. 1003-1017
    • Peters, P.1    Hsu, V.2    Ooi, C.3
  • 169
    • 0034700364 scopus 로고    scopus 로고
    • Molecular aspects of the cellular activities of ADP-ribosylation factors
    • Randazzo P, Nie Z, Miura K, Hsu V. Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci STKE 2000; 59: RE1.
    • (2000) Sci. STKE , vol.59
    • Randazzo, P.1    Nie, Z.2    Miura, K.3    Hsu, V.4
  • 170
    • 0034947806 scopus 로고    scopus 로고
    • Adp-ribosylation factor 6 delineates separate pathways used by endothelin 1 and insulin for stimulating glucose uptake in 3T3-L1 adipocytes
    • Lawrence J, Birnbaum M. Adp-ribosylation factor 6 delineates separate pathways used by endothelin 1 and insulin for stimulating glucose uptake in 3T3-L1 adipocytes. Mol Cell Biol. 2001; 15: 5276-5285.
    • (2001) Mol. Cell. Biol , vol.15 , pp. 5276-5285
    • Lawrence, J.1    Birnbaum, M.2
  • 172
    • 0034695624 scopus 로고    scopus 로고
    • Pantophysin is a phosphoprotein component of adipocyte transport vesicles and associates with GLUT4-containing vesicles
    • Brooks C, Scherer P, Cleveland K, Whittemore J, Lodish H, 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.1    Scherer, P.2    Cleveland, K.3    Whittemore, J.4    Lodish, H.5    Cheatham, B.6
  • 173
    • 0034680874 scopus 로고    scopus 로고
    • Cellugyrin is a marker for a distinct population of intracellular Glut4-containing vesicles
    • Kupriyanova T, Kandror K. Cellugyrin is a marker for a distinct population of intracellular Glut4-containing vesicles. J Biol Chem 2000; 275: 36263-36268.
    • (2000) J. Biol. Chem , vol.275 , pp. 36263-36268
    • Kupriyanova, T.1    Kandror, K.2
  • 174
    • 0037088655 scopus 로고    scopus 로고
    • Isolation and characterization of the two major intracellular Glut4 storage compartments
    • Kupriyanova T, Kandror V, Kandror K. Isolation and characterization of the two major intracellular Glut4 storage compartments. J Biol Chem 2002; 277: 9133-9138.
    • (2002) J. Biol. Chem , vol.277 , pp. 9133-9138
    • Kupriyanova, T.1    Kandror, V.2    Kandror, K.3


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