메뉴 건너뛰기




Volumn 70, Issue 16, 2013, Pages 2815-2834

Novel roles for insulin receptor (IR) in adipocytes and skeletal muscle cells via new and unexpected substrates

Author keywords

Adipose tissue; Insulin receptor; Insulin receptor substrate; Insulin signaling; Longevity; Metabolism; Mitogenesis; Skeletal muscle

Indexed keywords

ADAPTOR PROTEIN; ADIPOSE PROTEIN 2; BINDING PROTEIN; CAVEOLIN 1; CAVEOLIN 3; CBL PROTEIN; CYCLIC AMP BINDING PROTEIN; GRB 2 ASSOCIATED BINDER 1 PROTEIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; JANUS KINASE 1; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; MUNC18 PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SHC; SIRTUIN; SNARE PROTEIN; SOMATOMEDIN RECEPTOR; STAT5B PROTEIN; TRANSCRIPTION FACTOR FOXO; UNCLASSIFIED DRUG;

EID: 84881134459     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1176-1     Document Type: Review
Times cited : (24)

References (250)
  • 1
    • 0015071405 scopus 로고
    • Insulin-receptor interactions in adipose tissue cells: Direct measurement and properties
    • 5288373 1:CAS:528:DyaE3MXkslWqtr4%3D 10.1073/pnas.68.6.1264
    • Cuatrecasas P (1971) Insulin-receptor interactions in adipose tissue cells: direct measurement and properties. Proc Natl Acad Sci USA 68:1264-1268
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 1264-1268
    • Cuatrecasas, P.1
  • 2
    • 0015240302 scopus 로고
    • The relationship between the insulin-binding capacity of fat cells and the cellular response to insulin. Studies with intact and trypsin-treated fat cells
    • 5127426 1:CAS:528:DyaE38XhtVGktg%3D%3D
    • Kono T, Barham FW (1971) The relationship between the insulin-binding capacity of fat cells and the cellular response to insulin. Studies with intact and trypsin-treated fat cells. J Biol Chem 246:6210-6216
    • (1971) J Biol Chem , vol.246 , pp. 6210-6216
    • Kono, T.1    Barham, F.W.2
  • 3
    • 0015103371 scopus 로고
    • Insulin receptors in the liver: Specific binding of (125 I) insulin to the plasma membrane and its relation to insulin bioactivity
    • 1:CAS:528:DyaE3MXlsVyis7c%3D 10.1073/pnas.68.8.1833 4331561
    • Freychet P, Roth J, Neville DM Jr (1971) Insulin receptors in the liver: specific binding of (125 I) insulin to the plasma membrane and its relation to insulin bioactivity. Proc Natl Acad Sci USA 68:1833-1837
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 1833-1837
    • Freychet, P.1    Roth, J.2    Neville, Jr.D.M.3
  • 4
    • 0020065416 scopus 로고
    • Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor
    • 7031900 1:CAS:528:DyaL38XpvVWhuw%3D%3D 10.1126/science.7031900
    • Kasuga M, Karlsson FA, Kahn CR (1982) Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor. Science 215:185-187
    • (1982) Science , vol.215 , pp. 185-187
    • Kasuga, M.1    Karlsson, F.A.2    Kahn, C.R.3
  • 5
    • 0020561710 scopus 로고
    • Biosynthesis and glycosylation of the insulin receptor. Evidence for a single polypeptide precursor of the two major subunits
    • 6411700 1:CAS:528:DyaL3sXltFKlsr8%3D
    • Hedo JA, Kahn CR, Hayashi M, Yamada KM, Kasuga M (1983) Biosynthesis and glycosylation of the insulin receptor. Evidence for a single polypeptide precursor of the two major subunits. J Biol Chem 258:10020-10026
    • (1983) J Biol Chem , vol.258 , pp. 10020-10026
    • Hedo, J.A.1    Kahn, C.R.2    Hayashi, M.3    Yamada, K.M.4    Kasuga, M.5
  • 6
    • 0021924895 scopus 로고
    • The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
    • 2859121 1:CAS:528:DyaL2MXktFOltLw%3D 10.1016/0092-8674(85)90334-4
    • Ebina Y, Ellis L, Jarnagin K, Edery M, Graf L, et al. (1985) The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell 40:747-758
    • (1985) Cell , vol.40 , pp. 747-758
    • Ebina, Y.1    Ellis, L.2    Jarnagin, K.3    Edery, M.4    Graf, L.5
  • 7
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • 2983222 1:CAS:528:DyaL2MXhs1Wgu7k%3D 10.1038/313756a0
    • Ullrich A, Bell JR, Chen EY, Herrera R, Petruzzelli LM, et al. (1985) Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 313:756-761
    • (1985) Nature , vol.313 , pp. 756-761
    • Ullrich, A.1    Bell, J.R.2    Chen, E.Y.3    Herrera, R.4    Petruzzelli, L.M.5
  • 8
    • 0020702372 scopus 로고
    • Insulin receptor: Evidence that it is a protein kinase
    • 6849137 1:CAS:528:DyaL3sXmsF2jsQ%3D%3D 10.1126/science.6849137
    • Roth RA, Cassel DJ (1983) Insulin receptor: evidence that it is a protein kinase. Science 219:299-301
    • (1983) Science , vol.219 , pp. 299-301
    • Roth, R.A.1    Cassel, D.J.2
  • 9
    • 0020417020 scopus 로고
    • Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta
    • 6294652 1:CAS:528:DyaL3sXhtF2jug%3D%3D 10.1073/pnas.79.22.6792
    • Petruzzelli LM, Ganguly S, Smith CJ, Cobb MH, Rubin CS, et al. (1982) Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta. Proc Natl Acad Sci USA 79:6792-6796
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6792-6796
    • Petruzzelli, L.M.1    Ganguly, S.2    Smith, C.J.3    Cobb, M.H.4    Rubin, C.S.5
  • 10
    • 0019908766 scopus 로고
    • Phosphorylation of the hepatic insulin receptor: Stimulating effect of insulin on intact cells and in a cell-free system
    • 6749547 10.1016/0014-5793(82)80094-X
    • Van Obberghen E, Kowalski A (1982) Phosphorylation of the hepatic insulin receptor: stimulating effect of insulin on intact cells and in a cell-free system. FEBS Lett 143:179-182
    • (1982) FEBS Lett , vol.143 , pp. 179-182
    • Van Obberghen, E.1    Kowalski, A.2
  • 11
    • 0020283776 scopus 로고
    • Insulin receptor phosphorylation in intact adipocytes and in a cell-free system
    • 6758783 1:STN:280:DyaL3s7gtVChug%3D%3D 10.1016/S0006-291X(82)80082-X
    • Haring HU, Kasuga M, Kahn CR (1982) Insulin receptor phosphorylation in intact adipocytes and in a cell-free system. Biochem Biophys Res Commun 108:1538-1545
    • (1982) Biochem Biophys Res Commun , vol.108 , pp. 1538-1545
    • Haring, H.U.1    Kasuga, M.2    Kahn, C.R.3
  • 12
    • 0345476725 scopus 로고
    • Phosphorylation activates the insulin receptor tyrosine protein kinase
    • 6574482 1:CAS:528:DyaL3sXksVyiu7o%3D 10.1073/pnas.80.11.3237
    • Rosen OM, Herrera R, Olowe Y, Petruzzelli LM, Cobb MH (1983) Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc Natl Acad Sci USA 80:3237-3240
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3237-3240
    • Rosen, O.M.1    Herrera, R.2    Olowe, Y.3    Petruzzelli, L.M.4    Cobb, M.H.5
  • 13
    • 0021321439 scopus 로고
    • Tyrosine phosphorylation of the insulin receptor beta subunit activates the receptor-associated tyrosine kinase activity
    • 6538876 1:CAS:528:DyaL2cXhvVKhtLg%3D
    • Yu KT, Czech MP (1984) Tyrosine phosphorylation of the insulin receptor beta subunit activates the receptor-associated tyrosine kinase activity. J Biol Chem 259:5277-5286
    • (1984) J Biol Chem , vol.259 , pp. 5277-5286
    • Yu, K.T.1    Czech, M.P.2
  • 14
    • 0023022750 scopus 로고
    • Autophosphorylation of the insulin receptor in vitro. Designation of phosphorylation sites and correlation with receptor kinase activation
    • 3745176 1:CAS:528:DyaL28Xls1GmsLg%3D
    • Herrera R, Rosen OM (1986) Autophosphorylation of the insulin receptor in vitro. Designation of phosphorylation sites and correlation with receptor kinase activation. J Biol Chem 261:11980-11985
    • (1986) J Biol Chem , vol.261 , pp. 11980-11985
    • Herrera, R.1    Rosen, O.M.2
  • 15
    • 0022589978 scopus 로고
    • Kinetic properties of the insulin receptor tyrosine protein kinase: Activation through an insulin-stimulated tyrosine-specific, intramolecular autophosphorylation
    • 3004334 1:CAS:528:DyaL28XhtVCqs70%3D 10.1016/0003-9861(86)90098-6
    • Kwok YC, Nemenoff RA, Powers AC, Avruch J (1986) Kinetic properties of the insulin receptor tyrosine protein kinase: activation through an insulin-stimulated tyrosine-specific, intramolecular autophosphorylation. Arch Biochem Biophys 244:102-113
    • (1986) Arch Biochem Biophys , vol.244 , pp. 102-113
    • Kwok, Y.C.1    Nemenoff, R.A.2    Powers, A.C.3    Avruch, J.4
  • 16
    • 0020582406 scopus 로고
    • The beta subunit of the insulin receptor is an insulin-activated protein kinase
    • 6340724 1:CAS:528:DyaL3sXmsFyksQ%3D%3D 10.1021/bi00273a001
    • Shia MA, Pilch PF (1983) The beta subunit of the insulin receptor is an insulin-activated protein kinase. Biochemistry 22:717-721
    • (1983) Biochemistry , vol.22 , pp. 717-721
    • Shia, M.A.1    Pilch, P.F.2
  • 17
    • 0021241353 scopus 로고
    • Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes
    • 6368559 1:CAS:528:DyaL2cXhs1yku78%3D
    • Ronnett GV, Knutson P, Kohanski RA, Simpson TL, Lane MD (1984) Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes. J Biol Chem 259:4566-4575
    • (1984) J Biol Chem , vol.259 , pp. 4566-4575
    • Ronnett, G.V.1    Knutson, P.2    Kohanski, R.A.3    Simpson, T.L.4    Lane, M.D.5
  • 18
    • 0024548162 scopus 로고
    • Structure of the human insulin receptor gene and characterization of its promoter
    • 2911561 1:CAS:528:DyaL1MXht12lsLc%3D 10.1073/pnas.86.1.114
    • Seino S, Seino M, Nishi S, Bell GI (1989) Structure of the human insulin receptor gene and characterization of its promoter. Proc Natl Acad Sci USA 86:114-118
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 114-118
    • Seino, S.1    Seino, M.2    Nishi, S.3    Bell, G.I.4
  • 19
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • 7997262 1:CAS:528:DyaK2MXisl2qu7o%3D 10.1038/372746a0
    • Hubbard SR, Wei L, Ellis L, Hendrickson WA (1994) Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372:746-754
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 20
    • 0242484309 scopus 로고
    • Isolation of a Drosophila genomic sequence homologous to the kinase domain of the human insulin receptor and detection of the phosphorylated Drosophila receptor with an anti-peptide antibody
    • 3014506 1:CAS:528:DyaL28XkvFagsLY%3D 10.1073/pnas.83.13.4710
    • Petruzzelli L, Herrera R, Arenas-Garcia R, Fernandez R, Birnbaum MJ, et al. (1986) Isolation of a Drosophila genomic sequence homologous to the kinase domain of the human insulin receptor and detection of the phosphorylated Drosophila receptor with an anti-peptide antibody. Proc Natl Acad Sci USA 83:4710-4714
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4710-4714
    • Petruzzelli, L.1    Herrera, R.2    Arenas-Garcia, R.3    Fernandez, R.4    Birnbaum, M.J.5
  • 21
    • 0022347547 scopus 로고
    • Insulin rapidly stimulates tyrosine phosphorylation of a mγ-185,000 protein in intact cells
    • 2414672 1:CAS:528:DyaL28XivFajtg%3D%3D 10.1038/318183a0
    • White MF, Maron R, Kahn CR (1985) Insulin rapidly stimulates tyrosine phosphorylation of a mγ-185,000 protein in intact cells. Nature 318:183-186
    • (1985) Nature , vol.318 , pp. 183-186
    • White, M.F.1    Maron, R.2    Kahn, C.R.3
  • 22
    • 0025837881 scopus 로고
    • Purification and partial sequence analysis of pp 185, the major cellular substrate of the insulin receptor tyrosine kinase
    • 2022647 1:CAS:528:DyaK3MXltlSmsr8%3D
    • Rothenberg PL, Lane WS, Karasik A, Backer J, White M, et al. (1991) Purification and partial sequence analysis of pp 185, the major cellular substrate of the insulin receptor tyrosine kinase. J Biol Chem 266:8302-8311
    • (1991) J Biol Chem , vol.266 , pp. 8302-8311
    • Rothenberg, P.L.1    Lane, W.S.2    Karasik, A.3    Backer, J.4    White, M.5
  • 23
    • 0025813375 scopus 로고
    • Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
    • 1648180 1:CAS:528:DyaK38Xit1ygur8%3D 10.1038/352073a0
    • Sun XJ, Rothenberg P, Kahn CR, Backer JM, Araki E, et al. (1991) Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature 352:73-77
    • (1991) Nature , vol.352 , pp. 73-77
    • Sun, X.J.1    Rothenberg, P.2    Kahn, C.R.3    Backer, J.M.4    Araki, E.5
  • 24
    • 0026793456 scopus 로고
    • Growth factor signaling by receptor tyrosine kinases
    • 1326293 1:CAS:528:DyaK38Xmt1Knsrw%3D 10.1016/0896-6273(92)90177-F
    • Schlessinger J, Ullrich A (1992) Growth factor signaling by receptor tyrosine kinases. Neuron 9:383-391
    • (1992) Neuron , vol.9 , pp. 383-391
    • Schlessinger, J.1    Ullrich, A.2
  • 25
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • 2158859 1:CAS:528:DyaK3cXktlKnu74%3D 10.1016/0092-8674(90)90801-K
    • Ullrich A, Schlessinger J (1990) Signal transduction by receptors with tyrosine kinase activity. Cell 61:203-212
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 26
    • 0025062397 scopus 로고
    • Human insulin-receptor gene
    • 2227119 1:CAS:528:DyaK3cXhtlehs7o%3D 10.2337/diabetes.39.2.129
    • Seino S, Seino M, Bell GI (1990) Human insulin-receptor gene. Diabetes 39:129-133
    • (1990) Diabetes , vol.39 , pp. 129-133
    • Seino, S.1    Seino, M.2    Bell, G.I.3
  • 27
    • 66249148986 scopus 로고    scopus 로고
    • Lineage-specific biology revealed by a finished genome assembly of the mouse
    • 19468303 10.1371/journal.pbio.1000112 1:CAS:528:DC%2BD1MXntV2rtLo%3D
    • Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, et al. (2009) Lineage-specific biology revealed by a finished genome assembly of the mouse. PLoS Biol 7:e1000112
    • (2009) PLoS Biol , vol.7 , pp. 1000112
    • Church, D.M.1    Goodstadt, L.2    Hillier, L.W.3    Zody, M.C.4    Goldstein, S.5
  • 28
    • 0021885387 scopus 로고
    • Gene for human insulin receptor: Localization to site on chromosome 19 involved in pre-B-cell leukemia
    • 3873110 1:CAS:528:DyaL2MXitFKhsb8%3D 10.1126/science.3873110
    • Yang-Feng TL, Francke U, Ullrich A (1985) Gene for human insulin receptor: localization to site on chromosome 19 involved in pre-B-cell leukemia. Science 228:728-731
    • (1985) Science , vol.228 , pp. 728-731
    • Yang-Feng, T.L.1    Francke, U.2    Ullrich, A.3
  • 29
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • 7821729 10.1007/BF00400837
    • De Meyts P (1994) The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling. Diabetologia 37:S135-S148
    • (1994) Diabetologia , vol.37
    • De Meyts, P.1
  • 30
    • 0028268592 scopus 로고
    • A model for insulin binding to the insulin receptor
    • 8181471 1:CAS:528:DyaK2cXkt1Oisrs%3D 10.1111/j.1432-1033.1994.tb18833.x
    • Schaffer L (1994) A model for insulin binding to the insulin receptor. Eur J Biochem 221:1127-1132
    • (1994) Eur J Biochem , vol.221 , pp. 1127-1132
    • Schaffer, L.1
  • 31
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • 12360255 10.1038/nrd917 1:CAS:528:DC%2BD38XnsVGru7g%3D
    • De Meyts P, Whittaker J (2002) Structural biology of insulin and IGF1 receptors: implications for drug design. Nat Rev Drug Discov 1:769-783
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 32
    • 34250306385 scopus 로고    scopus 로고
    • Complementation analysis demonstrates that insulin cross-links both alpha subunits in a truncated insulin receptor dimer
    • 17339314 1:CAS:528:DC%2BD2sXks1Gns78%3D 10.1074/jbc.M700724200
    • Chan SJ, Nakagawa S, Steiner DF (2007) Complementation analysis demonstrates that insulin cross-links both alpha subunits in a truncated insulin receptor dimer. J Biol Chem 282:13754-13758
    • (2007) J Biol Chem , vol.282 , pp. 13754-13758
    • Chan, S.J.1    Nakagawa, S.2    Steiner, D.F.3
  • 33
    • 0031036850 scopus 로고    scopus 로고
    • Conformational changes of the insulin receptor upon insulin binding and activation as monitored by fluorescence spectroscopy
    • 9054578 1:CAS:528:DyaK2sXitFSrt7w%3D 10.1021/bi961815g
    • Lee J, Pilch PF, Shoelson SE, Scarlata SF (1997) Conformational changes of the insulin receptor upon insulin binding and activation as monitored by fluorescence spectroscopy. Biochemistry 36:2701-2708
    • (1997) Biochemistry , vol.36 , pp. 2701-2708
    • Lee, J.1    Pilch, P.F.2    Shoelson, S.E.3    Scarlata, S.F.4
  • 34
    • 77951058594 scopus 로고    scopus 로고
    • Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists
    • 20348418 1:CAS:528:DC%2BC3cXltFSjtb0%3D 10.1073/pnas.1001813107
    • Smith BJ, Huang K, Kong G, Chan SJ, Nakagawa S, et al. (2010) Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists. Proc Natl Acad Sci USA 107:6771-6776
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 6771-6776
    • Smith, B.J.1    Huang, K.2    Kong, G.3    Chan, S.J.4    Nakagawa, S.5
  • 35
    • 78650954923 scopus 로고    scopus 로고
    • Structural and biological properties of the Drosophila insulin-like peptide 5 show evolutionary conservation
    • 20974844 1:CAS:528:DC%2BC3MXmvVeq 10.1074/jbc.M110.156018
    • Sajid W, Kulahin N, Schluckebier G, Ribel U, Henderson HR, et al. (2011) Structural and biological properties of the Drosophila insulin-like peptide 5 show evolutionary conservation. J Biol Chem 286:661-673
    • (2011) J Biol Chem , vol.286 , pp. 661-673
    • Sajid, W.1    Kulahin, N.2    Schluckebier, G.3    Ribel, U.4    Henderson, H.R.5
  • 36
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor
    • 2449432 1:CAS:528:DyaL1cXhsVKisLw%3D
    • White MF, Shoelson SE, Keutmann H, Kahn CR (1988) A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor. J Biol Chem 263:2969-2980
    • (1988) J Biol Chem , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4
  • 37
    • 0026470979 scopus 로고
    • The insulin receptor activation process involves localized conformational changes
    • 1331080 1:CAS:528:DyaK38XlvVGjsbs%3D
    • Baron V, Kaliman P, Gautier N, Van Obberghen E (1992) The insulin receptor activation process involves localized conformational changes. J Biol Chem 267:23290-23294
    • (1992) J Biol Chem , vol.267 , pp. 23290-23294
    • Baron, V.1    Kaliman, P.2    Gautier, N.3    Van Obberghen, E.4
  • 38
    • 0020457746 scopus 로고
    • The structure of insulin receptor and its subunits. Evidence for multiple nonreduced forms and a 210,000 possible proreceptor
    • 7107610 1:CAS:528:DyaL38XlsVSmsbc%3D
    • Kasuga M, Hedo JA, Yamada KM, Kahn CR (1982) The structure of insulin receptor and its subunits. Evidence for multiple nonreduced forms and a 210,000 possible proreceptor. J Biol Chem 257:10392-10399
    • (1982) J Biol Chem , vol.257 , pp. 10392-10399
    • Kasuga, M.1    Hedo, J.A.2    Yamada, K.M.3    Kahn, C.R.4
  • 39
    • 0022357827 scopus 로고
    • Insulin receptor internalization and recycling: Mechanism and significance
    • 3907718 1:CAS:528:DyaL28XhtVamtbs%3D 10.1016/S0300-9084(85)80112-7
    • Carpentier JL, Fehlmann M, Van Obberghen E, Gorden P, Orci L (1985) Insulin receptor internalization and recycling: mechanism and significance. Biochimie 67:1143-1145
    • (1985) Biochimie , vol.67 , pp. 1143-1145
    • Carpentier, J.L.1    Fehlmann, M.2    Van Obberghen, E.3    Gorden, P.4    Orci, L.5
  • 40
    • 67650146154 scopus 로고    scopus 로고
    • Rapid insulin-dependent endocytosis of the insulin receptor by caveolae in primary adipocytes
    • 19543529 10.1371/journal.pone.0005985 1:CAS:528:DC%2BD1MXnvVSjurs%3D
    • Fagerholm S, Ortegren U, Karlsson M, Ruishalme I, Stralfors P (2009) Rapid insulin-dependent endocytosis of the insulin receptor by caveolae in primary adipocytes. PLoS ONE 4:e5985
    • (2009) PLoS ONE , vol.4 , pp. 5985
    • Fagerholm, S.1    Ortegren, U.2    Karlsson, M.3    Ruishalme, I.4    Stralfors, P.5
  • 41
    • 0026765431 scopus 로고
    • Internalization of the human insulin receptor the insulin-independent pathway
    • 1618809 1:CAS:528:DyaK38Xks1ensL8%3D
    • Paccaud JP, Siddle K, Carpentier JL (1992) Internalization of the human insulin receptor the insulin-independent pathway. J Biol Chem 267:13101-13106
    • (1992) J Biol Chem , vol.267 , pp. 13101-13106
    • Paccaud, J.P.1    Siddle, K.2    Carpentier, J.L.3
  • 42
    • 0021999827 scopus 로고
    • Ultrastructural analysis of the organization and distribution of insulin receptors on the surface of 3T3-L1 adipocytes: Rapid microaggregation and migration of occupied receptors
    • 3920228 1:CAS:528:DyaL2MXhvFynsr0%3D 10.1002/jcp.1041230204
    • Smith RM, Cobb MH, Rosen OM, Jarett L (1985) Ultrastructural analysis of the organization and distribution of insulin receptors on the surface of 3T3-L1 adipocytes: rapid microaggregation and migration of occupied receptors. J Cell Physiol 123:167-179
    • (1985) J Cell Physiol , vol.123 , pp. 167-179
    • Smith, R.M.1    Cobb, M.H.2    Rosen, O.M.3    Jarett, L.4
  • 43
    • 0030693249 scopus 로고    scopus 로고
    • Insulin receptor/IGF-I receptor hybrids are widely distributed in mammalian tissues: Quantification of individual receptor species by selective immunoprecipitation and immunoblotting
    • 9355755 1:CAS:528:DyaK2sXmvVGktrw%3D
    • Bailyes EM, Nave BT, Soos MA, Orr SR, Hayward AC, et al. (1997) Insulin receptor/IGF-I receptor hybrids are widely distributed in mammalian tissues: quantification of individual receptor species by selective immunoprecipitation and immunoblotting. Biochem J 327(Pt 1):209-215
    • (1997) Biochem J , vol.327 , Issue.PART 1 , pp. 209-215
    • Bailyes, E.M.1    Nave, B.T.2    Soos, M.A.3    Orr, S.R.4    Hayward, A.C.5
  • 44
    • 0032745869 scopus 로고    scopus 로고
    • Localization of the insulin receptor in caveolae of adipocyte plasma membrane
    • 10544179 1:CAS:528:DyaK1MXnt1Gntbs%3D
    • Gustavsson J, Parpal S, Karlsson M, Ramsing C, Thorn H, et al. (1999) Localization of the insulin receptor in caveolae of adipocyte plasma membrane. FASEB J 13:1961-1971
    • (1999) FASEB J , vol.13 , pp. 1961-1971
    • Gustavsson, J.1    Parpal, S.2    Karlsson, M.3    Ramsing, C.4    Thorn, H.5
  • 45
    • 33846615966 scopus 로고    scopus 로고
    • The neck of caveolae is a distinct plasma membrane subdomain that concentrates insulin receptors in 3T3-L1 adipocytes
    • 17227843 1:CAS:528:DC%2BD2sXht1yrurY%3D 10.1073/pnas.0610523104
    • Foti M, Porcheron G, Fournier M, Maeder C, Carpentier JL (2007) The neck of caveolae is a distinct plasma membrane subdomain that concentrates insulin receptors in 3T3-L1 adipocytes. Proc Natl Acad Sci USA 104:1242-1247
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1242-1247
    • Foti, M.1    Porcheron, G.2    Fournier, M.3    Maeder, C.4    Carpentier, J.L.5
  • 46
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane
    • 9488658 1:CAS:528:DyaK1cXhslejsbc%3D 10.1074/jbc.273.10.5419
    • Okamoto T, Schlegel A, Scherer PE, Lisanti MP (1998) Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane. J Biol Chem 273:5419-5422
    • (1998) J Biol Chem , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 47
    • 0024403208 scopus 로고
    • Tissue-specific expression of two alternatively spliced insulin receptor mRNAs in man
    • 1:CAS:528:DyaL1MXls1yntb8%3D 10.1210/mend-3-8-1263
    • Moller DE, Yokata A, Caro JF, Flier JS (1989) Tissue-specific expression of two alternatively spliced insulin receptor mRNAs in man. Mol Endo 3:1263-1269
    • (1989) Mol Endo , vol.3 , pp. 1263-1269
    • Moller, D.E.1    Yokata, A.2    Caro, J.F.3    Flier, J.S.4
  • 48
    • 0024539198 scopus 로고
    • Alternative splicing of human insulin receptor messenger RNA
    • 2538124 1:CAS:528:DyaL1MXhs1Ogsbo%3D 10.1016/0006-291X(89)92439-X
    • Seino S, Bell GI (1989) Alternative splicing of human insulin receptor messenger RNA. Biochem Biophys Res Commun 159:312-316
    • (1989) Biochem Biophys Res Commun , vol.159 , pp. 312-316
    • Seino, S.1    Bell, G.I.2
  • 49
    • 0347993701 scopus 로고    scopus 로고
    • Isoform-specific insulin receptor signaling involves different plasma membrane domains
    • 14691140 1:CAS:528:DC%2BD2cXhslWn 10.1083/jcb.200306093
    • Uhles S, Moede T, Leibiger B, Berggren PO, Leibiger IB (2003) Isoform-specific insulin receptor signaling involves different plasma membrane domains. J Cell Biol 163:1327-1337
    • (2003) J Cell Biol , vol.163 , pp. 1327-1337
    • Uhles, S.1    Moede, T.2    Leibiger, B.3    Berggren, P.O.4    Leibiger, I.B.5
  • 50
    • 0032932822 scopus 로고    scopus 로고
    • Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells
    • 10207053 1:CAS:528:DyaK1MXislSltLk%3D
    • Frasca F, Pandini G, Scalia P, Sciacca L, Mineo R, et al. (1999) Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells. Mol Cell Biol 19:3278-3288
    • (1999) Mol Cell Biol , vol.19 , pp. 3278-3288
    • Frasca, F.1    Pandini, G.2    Scalia, P.3    Sciacca, L.4    Mineo, R.5
  • 51
    • 5044227353 scopus 로고    scopus 로고
    • Structural determinants for high-affinity binding of insulin-like growth factor II to insulin receptor (IR)-A, the exon 11 minus isoform of the IR
    • 15205474 1:CAS:528:DC%2BD2cXotFamsbg%3D 10.1210/me.2004-0183
    • Denley A, Bonython ER, Booker GW, Cosgrove LJ, Forbes BE, et al. (2004) Structural determinants for high-affinity binding of insulin-like growth factor II to insulin receptor (IR)-A, the exon 11 minus isoform of the IR. Mol Endocrinol 18:2502-2512
    • (2004) Mol Endocrinol , vol.18 , pp. 2502-2512
    • Denley, A.1    Bonython, E.R.2    Booker, G.W.3    Cosgrove, L.J.4    Forbes, B.E.5
  • 52
    • 0027537050 scopus 로고
    • Ligand-binding properties of the 2 isoforms of the human insulin receptor
    • 8440175 1:CAS:528:DyaK3sXhvVeqt7s%3D 10.1210/en.132.3.1132
    • Yamaguchi Y, Flier JS, Benecke H, Ransil BJ, Moller DE (1993) Ligand-binding properties of the 2 isoforms of the human insulin receptor. Endocrinology 132:1132-1138
    • (1993) Endocrinology , vol.132 , pp. 1132-1138
    • Yamaguchi, Y.1    Flier, J.S.2    Benecke, H.3    Ransil, B.J.4    Moller, D.E.5
  • 53
    • 70849120946 scopus 로고    scopus 로고
    • Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease
    • 19752219 1:CAS:528:DC%2BD1MXhsVyhsrbK 10.1210/er.2008-0047
    • Belfiore A, Frasca F, Pandini G, Sciacca L, Vigneri R (2009) Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease. Endocr Rev 30:586-623
    • (2009) Endocr Rev , vol.30 , pp. 586-623
    • Belfiore, A.1    Frasca, F.2    Pandini, G.3    Sciacca, L.4    Vigneri, R.5
  • 54
    • 0026500524 scopus 로고
    • Protein-tyrosine phosphatases and the regulation of insulin action
    • 1316360 1:CAS:528:DyaK38XpvFCgsg%3D%3D 10.1002/jcb.240480107
    • Goldstein BJ (1992) Protein-tyrosine phosphatases and the regulation of insulin action. J Cell Biochem 48:33-42
    • (1992) J Cell Biochem , vol.48 , pp. 33-42
    • Goldstein, B.J.1
  • 55
    • 0019877197 scopus 로고
    • Selective dephosphorylation of proteins containing phosphotyrosine by alkaline phosphatases
    • 6167574 1:CAS:528:DyaL3MXltFSrurk%3D
    • Swarup G, Cohen S, Garbers DL (1981) Selective dephosphorylation of proteins containing phosphotyrosine by alkaline phosphatases. J Biol Chem 256:8197-8201
    • (1981) J Biol Chem , vol.256 , pp. 8197-8201
    • Swarup, G.1    Cohen, S.2    Garbers, D.L.3
  • 56
    • 23044493861 scopus 로고    scopus 로고
    • Variants of ENPP1 are associated with childhood and adult obesity and increase the risk of glucose intolerance and type 2 diabetes
    • 16025115 1:CAS:528:DC%2BD2MXmsFKls74%3D 10.1038/ng1604
    • Meyre D, Bouatia-Naji N, Tounian A, Samson C, Lecoeur C, et al. (2005) Variants of ENPP1 are associated with childhood and adult obesity and increase the risk of glucose intolerance and type 2 diabetes. Nat Genet 37:863-867
    • (2005) Nat Genet , vol.37 , pp. 863-867
    • Meyre, D.1    Bouatia-Naji, N.2    Tounian, A.3    Samson, C.4    Lecoeur, C.5
  • 57
    • 0034127077 scopus 로고    scopus 로고
    • Decreased insulin receptor tyrosine kinase activity and plasma cell membrane glycoprotein-1 overexpression in skeletal muscle from obese women with gestational diabetes mellitus (GDM): Evidence for increased serine/threonine phosphorylation in pregnancy and GDM
    • 10871198 1:CAS:528:DC%2BD3cXisFylsLg%3D 10.2337/diabetes.49.4.603
    • Shao J, Catalano PM, Yamashita H, Ruyter I, Smith S, et al. (2000) Decreased insulin receptor tyrosine kinase activity and plasma cell membrane glycoprotein-1 overexpression in skeletal muscle from obese women with gestational diabetes mellitus (GDM): evidence for increased serine/threonine phosphorylation in pregnancy and GDM. Diabetes 49:603-610
    • (2000) Diabetes , vol.49 , pp. 603-610
    • Shao, J.1    Catalano, P.M.2    Yamashita, H.3    Ruyter, I.4    Smith, S.5
  • 58
    • 0036328567 scopus 로고    scopus 로고
    • Improved insulin sensitivity and resistance to weight gain in mice null for the Ahsg gene
    • 12145157 1:CAS:528:DC%2BD38XlvFKiu74%3D 10.2337/diabetes.51.8.2450
    • Mathews ST, Singh GP, Ranalletta M, Cintron VJ, Qiang X, et al. (2002) Improved insulin sensitivity and resistance to weight gain in mice null for the Ahsg gene. Diabetes 51:2450-2458
    • (2002) Diabetes , vol.51 , pp. 2450-2458
    • Mathews, S.T.1    Singh, G.P.2    Ranalletta, M.3    Cintron, V.J.4    Qiang, X.5
  • 59
    • 0035970744 scopus 로고    scopus 로고
    • The BPS domain of Grb10 inhibits the catalytic activity of the insulin and IGF1 receptors
    • 11287005 1:CAS:528:DC%2BD3MXitl2itLo%3D 10.1016/S0014-5793(01)02282-7
    • Stein EG, Gustafson TA, Hubbard SR (2001) The BPS domain of Grb10 inhibits the catalytic activity of the insulin and IGF1 receptors. FEBS Lett 493:106-111
    • (2001) FEBS Lett , vol.493 , pp. 106-111
    • Stein, E.G.1    Gustafson, T.A.2    Hubbard, S.R.3
  • 60
    • 34548779732 scopus 로고    scopus 로고
    • Peripheral disruption of the Grb10 gene enhances insulin signaling and sensitivity in vivo
    • 17620412 1:CAS:528:DC%2BD2sXhtVKls7nK 10.1128/MCB.00679-07
    • Wang L, Balas B, Christ-Roberts CY, Kim RY, Ramos FJ, et al. (2007) Peripheral disruption of the Grb10 gene enhances insulin signaling and sensitivity in vivo. Mol Cell Biol 27:6497-6505
    • (2007) Mol Cell Biol , vol.27 , pp. 6497-6505
    • Wang, L.1    Balas, B.2    Christ-Roberts, C.Y.3    Kim, R.Y.4    Ramos, F.J.5
  • 61
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • 10066179 1:CAS:528:DyaK1MXhs1ymtrs%3D 10.1126/science.283.5407.1544
    • Elchebly M, Payette P, Michaliszyn E, Cromlish W, Collins S, et al. (1999) Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283:1544-1548
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3    Cromlish, W.4    Collins, S.5
  • 62
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • 10891488 1:CAS:528:DC%2BD3cXlt1Sntbs%3D 10.1128/MCB.20.15.5479-5489.2000
    • Klaman LD, Boss O, Peroni OD, Kim JK, Martino JL, et al. (2000) Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol Cell Biol 20:5479-5489
    • (2000) Mol Cell Biol , vol.20 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3    Kim, J.K.4    Martino, J.L.5
  • 63
    • 33746810001 scopus 로고    scopus 로고
    • Neuronal PTP1B regulates body weight, adiposity and leptin action
    • 16845389 1:CAS:528:DC%2BD28Xnsl2iur4%3D 10.1038/nm1435
    • Bence KK, Delibegovic M, Xue B, Gorgun CZ, Hotamisligil GS, et al. (2006) Neuronal PTP1B regulates body weight, adiposity and leptin action. Nat Med 12:917-924
    • (2006) Nat Med , vol.12 , pp. 917-924
    • Bence, K.K.1    Delibegovic, M.2    Xue, B.3    Gorgun, C.Z.4    Hotamisligil, G.S.5
  • 64
    • 1542285112 scopus 로고    scopus 로고
    • Modulation of insulin action
    • 14722654 1:CAS:528:DC%2BD2cXjtFCktb4%3D 10.1007/s00125-003-1313-3
    • Pirola L, Johnston AM, Van Obberghen E (2004) Modulation of insulin action. Diabetologia 47:170-184
    • (2004) Diabetologia , vol.47 , pp. 170-184
    • Pirola, L.1    Johnston, A.M.2    Van Obberghen, E.3
  • 65
    • 0344305782 scopus 로고    scopus 로고
    • Insulin signaling in health and disease
    • 14657487 1:CAS:528:DC%2BD3sXpsVWns7s%3D 10.1126/science.1092952
    • White MF (2003) Insulin signaling in health and disease. Science 302:1710-1711
    • (2003) Science , vol.302 , pp. 1710-1711
    • White, M.F.1
  • 66
    • 0018899124 scopus 로고
    • Role of insulin receptors in insulin-resistant states
    • 6990180 1:CAS:528:DyaL3cXitFejtrw%3D 10.1016/0026-0495(80)90171-7
    • Kahn CR (1980) Role of insulin receptors in insulin-resistant states. Metabolism 29:455-466
    • (1980) Metabolism , vol.29 , pp. 455-466
    • Kahn, C.R.1
  • 67
    • 0019639084 scopus 로고
    • Qualitative abnormalities in insulin binding in a patient with extreme insulin resistance: Decreased sensitivity to alterations in temperature and pH
    • 7031672 1:CAS:528:DyaL38XhvVaitw%3D%3D 10.1073/pnas.78.11.7157
    • Taylor SI, Roth J, Blizzard RM, Elders MJ (1981) Qualitative abnormalities in insulin binding in a patient with extreme insulin resistance: decreased sensitivity to alterations in temperature and pH. Proc Natl Acad Sci USA 78:7157-7161
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7157-7161
    • Taylor, S.I.1    Roth, J.2    Blizzard, R.M.3    Elders, M.J.4
  • 68
    • 0018778991 scopus 로고
    • Downregulation of insulin receptors in obese man
    • 437366 1:CAS:528:DyaE1MXktleisbc%3D 10.2337/diabetes.28.4.287
    • Wigand JP, Blackard WG (1979) Downregulation of insulin receptors in obese man. Diabetes 28:287-291
    • (1979) Diabetes , vol.28 , pp. 287-291
    • Wigand, J.P.1    Blackard, W.G.2
  • 69
    • 0023120916 scopus 로고
    • Decreased kinase activity of insulin receptors from adipocytes of non-insulin-dependent diabetic subjects
    • 3540010 1:CAS:528:DyaL2sXmsFaqsg%3D%3D 10.1172/JCI112789
    • Freidenberg GR, Henry RR, Klein HH, Reichart DR, Olefsky JM (1987) Decreased kinase activity of insulin receptors from adipocytes of non-insulin-dependent diabetic subjects. J Clin Invest 79:240-250
    • (1987) J Clin Invest , vol.79 , pp. 240-250
    • Freidenberg, G.R.1    Henry, R.R.2    Klein, H.H.3    Reichart, D.R.4    Olefsky, J.M.5
  • 70
    • 0023222361 scopus 로고
    • Insulin receptor kinase in human skeletal muscle from obese subjects with and without noninsulin-dependent diabetes
    • 3033021 1:CAS:528:DyaL2sXkt1Wmtro%3D 10.1172/JCI112958
    • Caro JF, Sinha MK, Raju SM, Ittoop O, Pories WJ, et al. (1987) Insulin receptor kinase in human skeletal muscle from obese subjects with and without noninsulin-dependent diabetes. J Clin Invest 79:1330-1337
    • (1987) J Clin Invest , vol.79 , pp. 1330-1337
    • Caro, J.F.1    Sinha, M.K.2    Raju, S.M.3    Ittoop, O.4    Pories, W.J.5
  • 71
    • 0023551819 scopus 로고
    • Insulin-receptor kinase activity of adipose tissue from morbidly obese humans with and without NIDDM
    • 3032715 1:STN:280:DyaL2s7ptFCgug%3D%3D 10.2337/diabetes.36.5.620
    • Sinha MK, Pories WJ, Flickinger EG, Meelheim D, Caro JF (1987) Insulin-receptor kinase activity of adipose tissue from morbidly obese humans with and without NIDDM. Diabetes 36:620-625
    • (1987) Diabetes , vol.36 , pp. 620-625
    • Sinha, M.K.1    Pories, W.J.2    Flickinger, E.G.3    Meelheim, D.4    Caro, J.F.5
  • 72
    • 0022415592 scopus 로고
    • Insulin receptor tyrosine kinase is defective in skeletal muscle of insulin-resistant obese mice
    • 3892304 10.1038/315676a0
    • Le Marchand-Brustel Y, Gremeaux T, Ballotti R, Van Obberghen E (1985) Insulin receptor tyrosine kinase is defective in skeletal muscle of insulin-resistant obese mice. Nature 315:676-679
    • (1985) Nature , vol.315 , pp. 676-679
    • Le Marchand-Brustel, Y.1    Gremeaux, T.2    Ballotti, R.3    Van Obberghen, E.4
  • 73
    • 0023240110 scopus 로고
    • Defective insulin receptor tyrosine kinase in human skeletal muscle in obesity and type 2 (non-insulin-dependent) diabetes mellitus
    • 2824266 1:STN:280:DyaL1c%2FlsF2rsA%3D%3D 10.1007/BF00292549
    • Arner P, Pollare T, Lithell H, Livingston JN (1987) Defective insulin receptor tyrosine kinase in human skeletal muscle in obesity and type 2 (non-insulin-dependent) diabetes mellitus. Diabetologia 30:437-440
    • (1987) Diabetologia , vol.30 , pp. 437-440
    • Arner, P.1    Pollare, T.2    Lithell, H.3    Livingston, J.N.4
  • 74
    • 0024321216 scopus 로고
    • A defective intramolecular autoactivation cascade may cause the reduced kinase activity of the skeletal muscle insulin receptor from patients with non-insulin-dependent diabetes mellitus
    • 2722845 1:CAS:528:DyaL1MXksFGisLc%3D
    • Obermaier-Kusser B, White MF, Pongratz DE, Su Z, Ermel B, et al. (1989) A defective intramolecular autoactivation cascade may cause the reduced kinase activity of the skeletal muscle insulin receptor from patients with non-insulin-dependent diabetes mellitus. J Biol Chem 264:9497-9504
    • (1989) J Biol Chem , vol.264 , pp. 9497-9504
    • Obermaier-Kusser, B.1    White, M.F.2    Pongratz, D.E.3    Su, Z.4    Ermel, B.5
  • 75
    • 0028079621 scopus 로고
    • Role of human skeletal muscle insulin receptor kinase in the in vivo insulin resistance of noninsulin-dependent diabetes mellitus and obesity
    • 8106637 1:STN:280:DyaK2c7kvFWmtw%3D%3D 10.1210/jc.78.2.471
    • Nolan JJ, Freidenberg G, Henry R, Reichart D, Olefsky JM (1994) Role of human skeletal muscle insulin receptor kinase in the in vivo insulin resistance of noninsulin-dependent diabetes mellitus and obesity. J Clin Endocrinol Metab 78:471-477
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 471-477
    • Nolan, J.J.1    Freidenberg, G.2    Henry, R.3    Reichart, D.4    Olefsky, J.M.5
  • 76
    • 0025832095 scopus 로고
    • Impaired autophosphorylation of insulin receptors from abdominal skeletal muscles in nonobese subjects with NIDDM
    • 1647993 1:STN:280:DyaK3M3osFamuw%3D%3D 10.2337/diabetes.40.7.815
    • Maegawa H, Shigeta Y, Egawa K, Kobayashi M (1991) Impaired autophosphorylation of insulin receptors from abdominal skeletal muscles in nonobese subjects with NIDDM. Diabetes 40:815-819
    • (1991) Diabetes , vol.40 , pp. 815-819
    • Maegawa, H.1    Shigeta, Y.2    Egawa, K.3    Kobayashi, M.4
  • 77
    • 0032848778 scopus 로고    scopus 로고
    • Impaired glucose transport and insulin receptor tyrosine phosphorylation in skeletal muscle from obese women with gestational diabetes
    • 10480612 1:CAS:528:DyaK1MXmtVaitLc%3D 10.2337/diabetes.48.9.1807
    • Friedman JE, Ishizuka T, Shao J, Huston L, Highman T, et al. (1999) Impaired glucose transport and insulin receptor tyrosine phosphorylation in skeletal muscle from obese women with gestational diabetes. Diabetes 48:1807-1814
    • (1999) Diabetes , vol.48 , pp. 1807-1814
    • Friedman, J.E.1    Ishizuka, T.2    Shao, J.3    Huston, L.4    Highman, T.5
  • 78
    • 0026490523 scopus 로고
    • Regulation of glucose transport in skeletal muscle
    • 1426762 1:CAS:528:DyaK3sXhvFOksw%3D%3D
    • Barnard RJ, Youngren JF (1992) Regulation of glucose transport in skeletal muscle. FASEB J 6:3238-3244
    • (1992) FASEB J , vol.6 , pp. 3238-3244
    • Barnard, R.J.1    Youngren, J.F.2
  • 79
    • 0031978984 scopus 로고    scopus 로고
    • Exercise, glucose transport, and insulin sensitivity
    • 9509261 1:CAS:528:DyaK1cXhtFKqs74%3D 10.1146/annurev.med.49.1.235
    • Goodyear LJ, Kahn BB (1998) Exercise, glucose transport, and insulin sensitivity. Annu Rev Med 49:235-261
    • (1998) Annu Rev Med , vol.49 , pp. 235-261
    • Goodyear, L.J.1    Kahn, B.B.2
  • 80
    • 3242714887 scopus 로고    scopus 로고
    • Clinical course of genetic diseases of the insulin receptor (type A and Rabson-Mendenhall syndromes): A 30-year prospective
    • 1:CAS:528:DC%2BD2cXltlOkurY%3D 10.1097/01.md.0000133625.73570.54
    • Musso C, Cochran E, Moran SA, Skarulis MC, Oral EA, et al. (2004) Clinical course of genetic diseases of the insulin receptor (type A and Rabson-Mendenhall syndromes): a 30-year prospective. Medicine (Baltimore) 83:209-222
    • (2004) Medicine (Baltimore) , vol.83 , pp. 209-222
    • Musso, C.1    Cochran, E.2    Moran, S.A.3    Skarulis, M.C.4    Oral, E.A.5
  • 81
    • 0027179476 scopus 로고
    • Homozygous deletion of the human insulin receptor gene results in Leprechaunism
    • 7693131 1:CAS:528:DyaK3sXmt1eht7o%3D 10.1038/ng0993-71
    • Wertheimer E, Lu SP, Backeljauw PF, Davenport ML, Taylor SI (1993) Homozygous deletion of the human insulin receptor gene results in Leprechaunism. Nat Genet 5:71-73
    • (1993) Nat Genet , vol.5 , pp. 71-73
    • Wertheimer, E.1    Lu, S.P.2    Backeljauw, P.F.3    Davenport, M.L.4    Taylor, S.I.5
  • 82
    • 0024289963 scopus 로고
    • Insulin resistance by unprocessed insulin proreceptors point mutation at the cleavage site
    • 3289535 1:CAS:528:DyaL1cXltVynsbY%3D 10.1016/S0006-291X(88)81145-8
    • Kobayashi M, Sasaoka T, Takata Y, Ishibashi O, Sugibayashi M, et al. (1988) Insulin resistance by unprocessed insulin proreceptors point mutation at the cleavage site. Biochem Biophys Res Commun 153:657-663
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 657-663
    • Kobayashi, M.1    Sasaoka, T.2    Takata, Y.3    Ishibashi, O.4    Sugibayashi, M.5
  • 83
    • 0034873099 scopus 로고    scopus 로고
    • Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy
    • 11528389 1:CAS:528:DC%2BD3MXmvFGmsbg%3D 10.1038/ng704
    • Savkur RS, Philips AV, Cooper TA (2001) Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy. Nat Genet 29:40-47
    • (2001) Nat Genet , vol.29 , pp. 40-47
    • Savkur, R.S.1    Philips, A.V.2    Cooper, T.A.3
  • 84
    • 0036118261 scopus 로고    scopus 로고
    • Clinical course of the syndrome of autoantibodies to the insulin receptor (type B insulin resistance): A 28-year perspective
    • 1:CAS:528:DC%2BD38Xis1alsbY%3D 10.1097/00005792-200203000-00001
    • Arioglu E, Andewelt A, Diabo C, Bell M, Taylor SI, et al. (2002) Clinical course of the syndrome of autoantibodies to the insulin receptor (type B insulin resistance): a 28-year perspective. Medicine (Baltimore) 81:87-100
    • (2002) Medicine (Baltimore) , vol.81 , pp. 87-100
    • Arioglu, E.1    Andewelt, A.2    Diabo, C.3    Bell, M.4    Taylor, S.I.5
  • 85
    • 0027322636 scopus 로고
    • Altered pattern of insulin receptor isotypes in skeletal muscle membranes of type 2 (non-insulin-dependent) diabetic subjects
    • 8359580 1:STN:280:DyaK3szms1SitA%3D%3D 10.1007/BF00404072
    • Kellerer M, Sesti G, Seffer E, Obermaier-Kusser B, Pongratz DE, et al. (1993) Altered pattern of insulin receptor isotypes in skeletal muscle membranes of type 2 (non-insulin-dependent) diabetic subjects. Diabetologia 36:628-632
    • (1993) Diabetologia , vol.36 , pp. 628-632
    • Kellerer, M.1    Sesti, G.2    Seffer, E.3    Obermaier-Kusser, B.4    Pongratz, D.E.5
  • 86
    • 13344277357 scopus 로고    scopus 로고
    • Early neonatal death in mice homozygous for a null allele of the insulin receptor gene
    • 8528241 1:CAS:528:DyaK28XhsV2gtg%3D%3D 10.1038/ng0196-106
    • Accili D, Drago J, Lee EJ, Johnson MD, Cool MH, et al. (1996) Early neonatal death in mice homozygous for a null allele of the insulin receptor gene. Nat Genet 12:106-109
    • (1996) Nat Genet , vol.12 , pp. 106-109
    • Accili, D.1    Drago, J.2    Lee, E.J.3    Johnson, M.D.4    Cool, M.H.5
  • 87
    • 0029879127 scopus 로고    scopus 로고
    • Targeted disruption of the insulin receptor gene in the mouse results in neonatal lethality
    • 8612577 1:CAS:528:DyaK28XisVOmtL0%3D
    • Joshi RL, Lamothe B, Cordonnier N, Mesbah K, Monthioux E, et al. (1996) Targeted disruption of the insulin receptor gene in the mouse results in neonatal lethality. EMBO J 15:1542-1547
    • (1996) EMBO J , vol.15 , pp. 1542-1547
    • Joshi, R.L.1    Lamothe, B.2    Cordonnier, N.3    Mesbah, K.4    Monthioux, E.5
  • 88
    • 0038155702 scopus 로고    scopus 로고
    • Development of a novel polygenic model of NIDDM in mice heterozygous for IR and IRS-1 null alleles
    • 9038347 1:STN:280:DyaK2s7ptVWqsA%3D%3D 10.1016/S0092-8674(00)81896-6
    • Bruning JC, Winnay J, Bonner-Weir S, Taylor SI, Accili D, et al. (1997) Development of a novel polygenic model of NIDDM in mice heterozygous for IR and IRS-1 null alleles. Cell 88:561-572
    • (1997) Cell , vol.88 , pp. 561-572
    • Bruning, J.C.1    Winnay, J.2    Bonner-Weir, S.3    Taylor, S.I.4    Accili, D.5
  • 89
    • 0033966768 scopus 로고    scopus 로고
    • Tissue-specific insulin resistance in mice with mutations in the insulin receptor, IRS-1, and IRS-2
    • 10642598 1:CAS:528:DC%2BD3cXltFemtQ%3D%3D 10.1172/JCI7917
    • Kido Y, Burks DJ, Withers D, Bruning JC, Kahn CR, et al. (2000) Tissue-specific insulin resistance in mice with mutations in the insulin receptor, IRS-1, and IRS-2. J Clin Invest 105:199-205
    • (2000) J Clin Invest , vol.105 , pp. 199-205
    • Kido, Y.1    Burks, D.J.2    Withers, D.3    Bruning, J.C.4    Kahn, C.R.5
  • 90
    • 0032214652 scopus 로고    scopus 로고
    • A muscle-specific insulin receptor knockout exhibits features of the metabolic syndrome of NIDDM without altering glucose tolerance
    • 9844629 1:CAS:528:DyaK1MXhtV2muw%3D%3D 10.1016/S1097-2765(00)80155-0
    • Bruning JC, Michael MD, Winnay JN, Hayashi T, Horsch D, et al. (1998) A muscle-specific insulin receptor knockout exhibits features of the metabolic syndrome of NIDDM without altering glucose tolerance. Mol Cell 2:559-569
    • (1998) Mol Cell , vol.2 , pp. 559-569
    • Bruning, J.C.1    Michael, M.D.2    Winnay, J.N.3    Hayashi, T.4    Horsch, D.5
  • 91
    • 0036068133 scopus 로고    scopus 로고
    • Adipose tissue selective insulin receptor knockout protects against obesity and obesity-related glucose intolerance
    • 12110165 1:CAS:528:DC%2BD38XlsFSms7s%3D 10.1016/S1534-5807(02)00199-5
    • Bluher M, Michael MD, Peroni OD, Ueki K, Carter N, et al. (2002) Adipose tissue selective insulin receptor knockout protects against obesity and obesity-related glucose intolerance. Dev Cell 3:25-38
    • (2002) Dev Cell , vol.3 , pp. 25-38
    • Bluher, M.1    Michael, M.D.2    Peroni, O.D.3    Ueki, K.4    Carter, N.5
  • 92
    • 0023633077 scopus 로고
    • Dissociation of in vitro sensitivities of glucose transport and antilipolysis to insulin in NIDDM
    • 3307452 1:CAS:528:DyaL2sXmtlCiur0%3D
    • Yki-Jarvinen H, Kubo K, Zawadzki J, Lillioja S, Young A, et al. (1987) Dissociation of in vitro sensitivities of glucose transport and antilipolysis to insulin in NIDDM. Am J Physiol 253:E300-E304
    • (1987) Am J Physiol , vol.253
    • Yki-Jarvinen, H.1    Kubo, K.2    Zawadzki, J.3    Lillioja, S.4    Young, A.5
  • 93
    • 0033696020 scopus 로고    scopus 로고
    • Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells
    • 11003568 1:CAS:528:DC%2BD3cXnsFOrs7s%3D
    • Foster LJ, Klip A (2000) Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells. Am J Physiol Cell Physiol 279:C877-C890
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Foster, L.J.1    Klip, A.2
  • 94
    • 0037942739 scopus 로고    scopus 로고
    • Extended longevity in mice lacking the insulin receptor in adipose tissue
    • 12543978 10.1126/science.1078223 1:CAS:528:DC%2BD3sXlsVartg%3D%3D
    • Bluher M, Kahn BB, Kahn CR (2003) Extended longevity in mice lacking the insulin receptor in adipose tissue. Science 299:572-574
    • (2003) Science , vol.299 , pp. 572-574
    • Bluher, M.1    Kahn, B.B.2    Kahn, C.R.3
  • 95
    • 0034783580 scopus 로고    scopus 로고
    • Brown adipose tissue-specific insulin receptor knockout shows diabetic phenotype without insulin resistance
    • 11602628 1:CAS:528:DC%2BD3MXns1ChsLo%3D
    • Guerra C, Navarro P, Valverde AM, Arribas M, Bruning J, et al. (2001) Brown adipose tissue-specific insulin receptor knockout shows diabetic phenotype without insulin resistance. J Clin Invest 108:1205-1213
    • (2001) J Clin Invest , vol.108 , pp. 1205-1213
    • Guerra, C.1    Navarro, P.2    Valverde, A.M.3    Arribas, M.4    Bruning, J.5
  • 96
    • 79952428530 scopus 로고    scopus 로고
    • Diabetes in mice with selective impairment of insulin action in Glut4-expressing tissues
    • 21266328 1:CAS:528:DC%2BC3MXktVKksL4%3D 10.2337/db10-1056
    • Lin HV, Ren H, Samuel VT, Lee HY, Lu TY, et al. (2011) Diabetes in mice with selective impairment of insulin action in Glut4-expressing tissues. Diabetes 60:700-709
    • (2011) Diabetes , vol.60 , pp. 700-709
    • Lin, H.V.1    Ren, H.2    Samuel, V.T.3    Lee, H.Y.4    Lu, T.Y.5
  • 97
    • 0038856677 scopus 로고
    • Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody stimulated glucose uptake and receptor kinase activity
    • 3101064 1:CAS:528:DyaL2sXhtFeqsL8%3D 10.1073/pnas.84.3.704
    • Ebina Y, Araki E, Taira M, Shimada F, Mori M, et al. (1987) Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody stimulated glucose uptake and receptor kinase activity. Proc Natl Acad Sci USA 84:704-708
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 704-708
    • Ebina, Y.1    Araki, E.2    Taira, M.3    Shimada, F.4    Mori, M.5
  • 98
    • 0031792118 scopus 로고    scopus 로고
    • Impaired glucose tolerance in mice with a targeted impairment of insulin action in muscle and adipose tissue
    • 9806552 1:CAS:528:DyaK1cXntFOhtLk%3D 10.1038/3112
    • Lauro D, Kido Y, Castle AL, Zarnowski MJ, Hayashi H, et al. (1998) Impaired glucose tolerance in mice with a targeted impairment of insulin action in muscle and adipose tissue. Nat Genet 20:294-298
    • (1998) Nat Genet , vol.20 , pp. 294-298
    • Lauro, D.1    Kido, Y.2    Castle, A.L.3    Zarnowski, M.J.4    Hayashi, H.5
  • 99
    • 18144391553 scopus 로고    scopus 로고
    • Estrogen, insulin, and dietary signals cooperatively regulate longevity signals to enhance resistance to oxidative stress in mice
    • 15713666 1:CAS:528:DC%2BD2MXjtleiu7o%3D 10.1074/jbc.M500924200
    • Baba T, Shimizu T, Suzuki Y, Ogawara M, Isono K, et al. (2005) Estrogen, insulin, and dietary signals cooperatively regulate longevity signals to enhance resistance to oxidative stress in mice. J Biol Chem 280:16417-16426
    • (2005) J Biol Chem , vol.280 , pp. 16417-16426
    • Baba, T.1    Shimizu, T.2    Suzuki, Y.3    Ogawara, M.4    Isono, K.5
  • 100
    • 79953218702 scopus 로고    scopus 로고
    • Reconstitution of insulin action in muscle, white adipose tissue, and brain of insulin receptor knock-out mice fails to rescue diabetes
    • 21239487 1:CAS:528:DC%2BC3MXjtFOitbs%3D 10.1074/jbc.M110.210807
    • Lin HV, Accili D (2011) Reconstitution of insulin action in muscle, white adipose tissue, and brain of insulin receptor knock-out mice fails to rescue diabetes. J Biol Chem 286:9797-9804
    • (2011) J Biol Chem , vol.286 , pp. 9797-9804
    • Lin, H.V.1    Accili, D.2
  • 101
    • 0008385878 scopus 로고
    • Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site
    • 6771756 1:CAS:528:DyaL3cXktlOkt7c%3D 10.1073/pnas.77.5.2542
    • Suzuki K, Kono T (1980) Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site. Proc Natl Acad Sci USA 77:2542-2545
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2542-2545
    • Suzuki, K.1    Kono, T.2
  • 102
    • 0018820017 scopus 로고
    • Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell. Apparent translocation of intracellular transport systems to the plasma membrane
    • 6989818 1:CAS:528:DyaL3cXks1Wqs7c%3D
    • Cushman SW, Wardzala LJ (1980) Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell. Apparent translocation of intracellular transport systems to the plasma membrane. J Biol Chem 255:4758-4762
    • (1980) J Biol Chem , vol.255 , pp. 4758-4762
    • Cushman, S.W.1    Wardzala, L.J.2
  • 103
    • 0030669618 scopus 로고    scopus 로고
    • Moving GLUT4: The biogenesis and trafficking of GLUT4 storage vesicles
    • 9356011 1:CAS:528:DyaK2sXntVKjurs%3D 10.2337/diabetes.46.11.1667
    • Rea S, James DE (1997) Moving GLUT4: the biogenesis and trafficking of GLUT4 storage vesicles. Diabetes 46:1667-1677
    • (1997) Diabetes , vol.46 , pp. 1667-1677
    • Rea, S.1    James, D.E.2
  • 104
    • 0034648794 scopus 로고    scopus 로고
    • CAP defines a second signalling pathway required for insulin-stimulated glucose transport [see comments]
    • 11001060 1:CAS:528:DC%2BD3cXmvVSmtb0%3D 10.1038/35025089
    • Baumann CA, Ribon V, Kanzaki M, Thurmond DC, Mora S, et al. (2000) CAP defines a second signalling pathway required for insulin-stimulated glucose transport [see comments]. Nature 407:202-207
    • (2000) Nature , vol.407 , pp. 202-207
    • Baumann, C.A.1    Ribon, V.2    Kanzaki, M.3    Thurmond, D.C.4    Mora, S.5
  • 105
    • 79955517215 scopus 로고    scopus 로고
    • Munc18c phosphorylation by the insulin receptor links cell signaling directly to SNARE exocytosis
    • 21444687 1:CAS:528:DC%2BC3MXkslamu7Y%3D 10.1083/jcb.201007176
    • Jewell JL, Oh E, Ramalingam L, Kalwat MA, Tagliabracci VS, et al. (2011) Munc18c phosphorylation by the insulin receptor links cell signaling directly to SNARE exocytosis. J Cell Biol 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
  • 106
    • 0025063340 scopus 로고
    • Glucose uptake in human and animal muscle cells in culture
    • 2188683 1:CAS:528:DyaK3cXhvFGktLw%3D 10.1139/o90-076
    • Sarabia V, Ramlal T, Klip A (1990) Glucose uptake in human and animal muscle cells in culture. Biochem Cell Biol 68:536-542
    • (1990) Biochem Cell Biol , vol.68 , pp. 536-542
    • Sarabia, V.1    Ramlal, T.2    Klip, A.3
  • 107
    • 0023131917 scopus 로고
    • Distribution of glucose transporters and insulin receptors in the plasma membrane and transverse tubules of skeletal muscle
    • 2949701 1:CAS:528:DyaL2sXps1Kgsg%3D%3D 10.1016/0003-9861(87)90661-8
    • Burdett E, Beeler T, Klip A (1987) Distribution of glucose transporters and insulin receptors in the plasma membrane and transverse tubules of skeletal muscle. Arch Biochem Biophys 253:279-286
    • (1987) Arch Biochem Biophys , vol.253 , pp. 279-286
    • Burdett, E.1    Beeler, T.2    Klip, A.3
  • 108
    • 0028947967 scopus 로고
    • Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter
    • 7829503 1:CAS:528:DyaK2MXjtlWqurg%3D 10.1074/jbc.270.5.1679
    • Hansen PA, Gulve EA, Marshall BA, Gao J, Pessin JE, et al. (1995) Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter. J Biol Chem 270:1679-1684
    • (1995) J Biol Chem , vol.270 , pp. 1679-1684
    • Hansen, P.A.1    Gulve, E.A.2    Marshall, B.A.3    Gao, J.4    Pessin, J.E.5
  • 109
    • 0029148591 scopus 로고
    • Role of IRS-2 in insulin and cytokine signalling
    • 7675087 1:CAS:528:DyaK2MXotVOhtLc%3D 10.1038/377173a0
    • Sun XJ, Wang LM, Zhang Y, Yenush L, Myers MG, et al. (1995) Role of IRS-2 in insulin and cytokine signalling. Nature 377:173-177
    • (1995) Nature , vol.377 , pp. 173-177
    • Sun, X.J.1    Wang, L.M.2    Zhang, Y.3    Yenush, L.4    Myers, M.G.5
  • 110
    • 21444460644 scopus 로고    scopus 로고
    • Differential contribution of insulin receptor substrates 1 versus 2 to insulin signaling and glucose uptake in l6 myotubes
    • 15764603 1:CAS:528:DC%2BD2MXjvFertro%3D 10.1074/jbc.M412317200
    • Huang C, Thirone AC, Huang X, Klip A (2005) Differential contribution of insulin receptor substrates 1 versus 2 to insulin signaling and glucose uptake in l6 myotubes. J Biol Chem 280:19426-19435
    • (2005) J Biol Chem , vol.280 , pp. 19426-19435
    • Huang, C.1    Thirone, A.C.2    Huang, X.3    Klip, A.4
  • 111
    • 0034682780 scopus 로고    scopus 로고
    • Essential role of insulin receptor substrate-2 in insulin stimulation of Glut4 translocation and glucose uptake in brown adipocytes
    • 10829031 1:CAS:528:DC%2BD3cXmtVehsLg%3D 10.1074/jbc.M004046200
    • Fasshauer M, Klein J, Ueki K, Kriauciunas KM, Benito M, et al. (2000) Essential role of insulin receptor substrate-2 in insulin stimulation of Glut4 translocation and glucose uptake in brown adipocytes. J Biol Chem 275:25494-25501
    • (2000) J Biol Chem , vol.275 , pp. 25494-25501
    • Fasshauer, M.1    Klein, J.2    Ueki, K.3    Kriauciunas, K.M.4    Benito, M.5
  • 112
    • 0037816152 scopus 로고    scopus 로고
    • Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/DOK5
    • 12730241 1:CAS:528:DC%2BD3sXlt1CmtL4%3D 10.1074/jbc.M212430200
    • Cai D, Dhe-Paganon S, Melendez PA, Lee J, Shoelson SE (2003) Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/DOK5. J Biol Chem 278:25323-25330
    • (2003) J Biol Chem , vol.278 , pp. 25323-25330
    • Cai, D.1    Dhe-Paganon, S.2    Melendez, P.A.3    Lee, J.4    Shoelson, S.E.5
  • 113
    • 0032941110 scopus 로고    scopus 로고
    • Cloning, tissue expression, and chromosomal location of the mouse insulin receptor substrate 4 gene
    • 10067860 1:CAS:528:DyaK1MXhsFCjurY%3D 10.1210/en.140.3.1329
    • Fantin VR, Lavan BE, Wang Q, Jenkins NA, Gilbert DJ, et al. (1999) Cloning, tissue expression, and chromosomal location of the mouse insulin receptor substrate 4 gene. Endocrinology 140:1329-1337
    • (1999) Endocrinology , vol.140 , pp. 1329-1337
    • Fantin, V.R.1    Lavan, B.E.2    Wang, Q.3    Jenkins, N.A.4    Gilbert, D.J.5
  • 114
    • 0026489451 scopus 로고
    • IRS-1 activates phosphatidylinositol 3′-kinase by associating with src homology 2 domains of p85
    • 1332046 1:CAS:528:DyaK3sXhs1Kntw%3D%3D 10.1073/pnas.89.21.10350
    • Myers MG, Backer JM, Sun XJ, Shoelson S, Hu P, et al. (1992) IRS-1 activates phosphatidylinositol 3′-kinase by associating with src homology 2 domains of p85. Proc Natl Acad Sci USA 89:10350-10354
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10350-10354
    • Myers, M.G.1    Backer, J.M.2    Sun, X.J.3    Shoelson, S.4    Hu, P.5
  • 115
    • 0034810894 scopus 로고    scopus 로고
    • Defects of the insulin receptor substrate (IRS) system in human metabolic disorders
    • 11641236 1:CAS:528:DC%2BD3MXnsV2msbw%3D 10.1096/fj.01-0009rev
    • Sesti G, Federici M, Hribal ML, Lauro D, Sbraccia P, et al. (2001) Defects of the insulin receptor substrate (IRS) system in human metabolic disorders. FASEB J 15:2099-2111
    • (2001) FASEB J , vol.15 , pp. 2099-2111
    • Sesti, G.1    Federici, M.2    Hribal, M.L.3    Lauro, D.4    Sbraccia, P.5
  • 116
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling
    • 9677303 1:CAS:528:DyaK1cXlsVWnsL4%3D
    • Shepherd PR, Withers DJ, Siddle K (1998) Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling. Biochem J 333(Pt 3):471-490
    • (1998) Biochem J , vol.333 , Issue.PART 3 , pp. 471-490
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 117
    • 1342342993 scopus 로고    scopus 로고
    • PDK1, the master regulator of AGC kinase signal transduction
    • 15209375 1:CAS:528:DC%2BD2cXhsFWlu7Y%3D 10.1016/j.semcdb.2003.12.022
    • Mora A, Komander D, van Aalten DM, Alessi DR (2004) PDK1, the master regulator of AGC kinase signal transduction. Semin Cell Dev Biol 15:161-170
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 161-170
    • Mora, A.1    Komander, D.2    Van Aalten, D.M.3    Alessi, D.R.4
  • 118
    • 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
    • 9819385 1:CAS:528:DyaK1cXnvVKlt7k%3D
    • Kotani K, Ogawa W, Matsumoto M, Kitamura T, Sakaue H, et al. (1998) Requirement of atypical protein kinase clambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes. Mol Cell Biol 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
  • 119
    • 1542781732 scopus 로고    scopus 로고
    • Isoform-specific regulation of insulin-dependent glucose uptake by Akt/protein kinase B
    • 14522993 1:CAS:528:DC%2BD3sXptlGrtL0%3D 10.1074/jbc.M306782200
    • Bae SS, Cho H, Mu J, Birnbaum MJ (2003) Isoform-specific regulation of insulin-dependent glucose uptake by Akt/protein kinase B. J Biol Chem 278:49530-49536
    • (2003) J Biol Chem , vol.278 , pp. 49530-49536
    • Bae, S.S.1    Cho, H.2    Mu, J.3    Birnbaum, M.J.4
  • 120
    • 0035448879 scopus 로고    scopus 로고
    • Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene
    • 11544177 1:CAS:528:DC%2BD3MXmvFSrurg%3D 10.1101/gad.913901
    • Chen WS, Xu PZ, Gottlob K, Chen ML, Sokol K, et al. (2001) Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene. Genes Dev 15:2203-2208
    • (2001) Genes Dev , vol.15 , pp. 2203-2208
    • Chen, W.S.1    Xu, P.Z.2    Gottlob, K.3    Chen, M.L.4    Sokol, K.5
  • 121
    • 26844573782 scopus 로고    scopus 로고
    • AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain
    • 15971998 1:CAS:528:DC%2BD2MXhtVehsL3E 10.1042/BJ20050887
    • Miinea CP, Sano H, Kane S, Sano E, Fukuda M, et al. (2005) AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain. Biochem J 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
  • 122
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • 12637568 1:CAS:528:DC%2BD3sXjtVCmt7w%3D 10.1074/jbc.C300063200
    • Sano H, Kane S, Sano E, Miinea CP, Asara JM, et al. (2003) Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J Biol Chem 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
  • 123
    • 0033913213 scopus 로고    scopus 로고
    • Signaling pathways in insulin action: Molecular targets of insulin resistance
    • 10903329 1:CAS:528:DC%2BD3cXkvFWhu7g%3D 10.1172/JCI10582
    • Pessin JE, Saltiel AR (2000) Signaling pathways in insulin action: molecular targets of insulin resistance. J Clin Invest 106:165-169
    • (2000) J Clin Invest , vol.106 , pp. 165-169
    • Pessin, J.E.1    Saltiel, A.R.2
  • 124
    • 0036098461 scopus 로고    scopus 로고
    • APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes
    • 11997497 1:CAS:528:DC%2BD38XjslWlsbw%3D 10.1128/MCB.22.11.3599-3609.2002
    • Liu J, Kimura A, Baumann CA, Saltiel AR (2002) APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes. Mol Cell Biol 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
  • 125
    • 0346156078 scopus 로고    scopus 로고
    • Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor
    • 14690593 1:CAS:528:DC%2BD2cXhsVOmug%3D%3D 10.1016/S1097-2765(03)00487-8
    • Hu J, Liu J, Ghirlando R, Saltiel AR, Hubbard SR (2003) Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Mol Cell 12:1379-1389
    • (2003) Mol Cell , vol.12 , pp. 1379-1389
    • Hu, J.1    Liu, J.2    Ghirlando, R.3    Saltiel, A.R.4    Hubbard, S.R.5
  • 126
    • 0031594145 scopus 로고    scopus 로고
    • A novel, multifunctional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes
    • 9447983 1:CAS:528:DyaK1cXltlGqtg%3D%3D
    • Ribon V, Printen JA, Hoffman NG, Kay BK, Saltiel AR (1998) A novel, multifunctional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes. Mol Cell Biol 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
  • 127
    • 18144396107 scopus 로고    scopus 로고
    • The stomatin/prohibitin/flotillin/HflK/C domain of flotillin-1 contains distinct sequences that direct plasma membrane localization and protein interactions in 3T3-L1 adipocytes
    • 15713660 1:CAS:528:DC%2BD2MXjtleit7c%3D 10.1074/jbc.M500940200
    • Liu J, Deyoung SM, Zhang M, Dold LH, Saltiel AR (2005) The stomatin/prohibitin/flotillin/HflK/C domain of flotillin-1 contains distinct sequences that direct plasma membrane localization and protein interactions in 3T3-L1 adipocytes. J Biol Chem 280:16125-16134
    • (2005) J Biol Chem , vol.280 , pp. 16125-16134
    • Liu, J.1    Deyoung, S.M.2    Zhang, M.3    Dold, L.H.4    Saltiel, A.R.5
  • 128
    • 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
    • 8524328 1:CAS:528:DyaK28XhtVGrsQ%3D%3D
    • Ribon V, Hubbell S, Herrera R, Saltiel AR (1996) The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner. Mol Cell Biol 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
  • 129
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
    • 7806500 1:CAS:528:DyaK2MXitFChu7s%3D
    • Knudsen BS, Feller SM, Hanafusa H (1994) Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk. J Biol Chem 269:32781-32787
    • (1994) J Biol Chem , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 130
    • 0035912228 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10
    • 11309621 1:CAS:528:DC%2BD3MXjt1Krt70%3D 10.1038/35073608
    • Chiang S-H, Baumann CA, Kanzaki M, Thurmond DC, Watson RT, et al. (2001) Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10. Nature 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
  • 131
    • 0035921433 scopus 로고    scopus 로고
    • Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation
    • 11502760 1:CAS:528:DC%2BD3MXmt1Shtro%3D 10.1083/jcb.200102078
    • Watson RT, Shigematsu S, Chiang SH, Mora S, Kanzaki M, et al. (2001) Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation. J Cell Biol 154:829-840
    • (2001) J Cell Biol , vol.154 , pp. 829-840
    • Watson, R.T.1    Shigematsu, S.2    Chiang, S.H.3    Mora, S.4    Kanzaki, M.5
  • 132
    • 0036790976 scopus 로고    scopus 로고
    • The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes
    • 12242347 1:CAS:528:DC%2BD38XnvFGhsbg%3D 10.1073/pnas.202495599
    • Chang L, Adams RD, Saltiel AR (2002) The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes. Proc Natl Acad Sci USA 99:12835-12840
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12835-12840
    • Chang, L.1    Adams, R.D.2    Saltiel, A.R.3
  • 133
    • 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
    • 10677349 1:CAS:528:DC%2BD3cXhvFSit78%3D 10.1042/0264-6021:3460321
    • Omata W, Shibata H, Li L, Takata K, Kojima I (2000) Actin filaments play a critical role in insulin-induced exocytotic recruitment but not in endocytosis of GLUT4 in isolated rat adipocytes. Biochem J 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
  • 134
    • 0028126854 scopus 로고
    • Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane
    • 7961991 1:CAS:528:DyaK2cXmslalsrc%3D
    • Tsakiridis T, Vranic M, Klip A (1994) Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane. J Biol Chem 269:29934-29942
    • (1994) J Biol Chem , vol.269 , pp. 29934-29942
    • Tsakiridis, T.1    Vranic, M.2    Klip, A.3
  • 135
    • 34249052338 scopus 로고    scopus 로고
    • Actin"g on GLUT4: Membrane and cytoskeletal components of insulin action
    • 18220662 1:CAS:528:DC%2BD2sXms1yhurc%3D 10.2174/157339907780598199
    • Brozinick JT Jr, Berkemeier BA, Elmendorf JS (2007) "Actin"g on GLUT4: membrane and cytoskeletal components of insulin action. Curr Diabetes Rev 3:111-122
    • (2007) Curr Diabetes Rev , vol.3 , pp. 111-122
    • Brozinick, Jr.J.T.1    Berkemeier, B.A.2    Elmendorf, J.S.3
  • 136
    • 0035834644 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling
    • 11546823 1:CAS:528:DC%2BD3MXosVGmsLk%3D 10.1074/jbc.M108297200
    • Kanzaki M, Pessin JE (2001) Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling. J Biol Chem 276:42436-42444
    • (2001) J Biol Chem , vol.276 , pp. 42436-42444
    • Kanzaki, M.1    Pessin, J.E.2
  • 137
    • 0033574585 scopus 로고    scopus 로고
    • Identification of the APS protein as a novel insulin receptor substrate [in process citation]
    • 10196204 1:CAS:528:DyaK1MXis1GmsbY%3D 10.1074/jbc.274.16.11186
    • Moodie SA, Alleman-Sposeto J, Gustafson TA (1999) Identification of the APS protein as a novel insulin receptor substrate [in process citation]. J Biol Chem 274:11186-11193
    • (1999) J Biol Chem , vol.274 , pp. 11186-11193
    • Moodie, S.A.1    Alleman-Sposeto, J.2    Gustafson, T.A.3
  • 138
    • 0030812414 scopus 로고    scopus 로고
    • Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation
    • 9233773 1:CAS:528:DyaK2sXkslygsb8%3D 10.1038/sj.onc.1201163
    • Yokouchi M, Suzuki R, Masuhara M, Komiya S, Inoue A, et al. (1997) Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation. Oncogene 15:7-15
    • (1997) Oncogene , vol.15 , pp. 7-15
    • Yokouchi, M.1    Suzuki, R.2    Masuhara, M.3    Komiya, S.4    Inoue, A.5
  • 139
    • 0034872381 scopus 로고    scopus 로고
    • Functional effects of APS and SH2-B on insulin receptor signalling
    • 11498022 1:CAS:528:DC%2BD3MXms1Sltrg%3D 10.1042/BST0290529
    • Ahmed Z, Pillay TS (2001) Functional effects of APS and SH2-B on insulin receptor signalling. Biochem Soc Trans 29:529-534
    • (2001) Biochem Soc Trans , vol.29 , pp. 529-534
    • Ahmed, Z.1    Pillay, T.S.2
  • 140
    • 0032189383 scopus 로고    scopus 로고
    • SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase
    • 9742218 1:CAS:528:DyaK1cXms1Ohu7w%3D
    • Kotani K, Wilden P, Pillay TS (1998) SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase. Biochem J 335(Pt 1):103-109
    • (1998) Biochem J , vol.335 , Issue.PART 1 , pp. 103-109
    • Kotani, K.1    Wilden, P.2    Pillay, T.S.3
  • 141
    • 24944515497 scopus 로고    scopus 로고
    • The interaction between the adaptor protein APS and Enigma is involved in actin organisation
    • 15946664 1:CAS:528:DC%2BD2MXmvVCht7k%3D 10.1016/j.yexcr.2005.05.008
    • Barres R, Gonzalez T, Le Marchand-Brustel Y, Tanti JF (2005) The interaction between the adaptor protein APS and Enigma is involved in actin organisation. Exp Cell Res 308:334-344
    • (2005) Exp Cell Res , vol.308 , pp. 334-344
    • Barres, R.1    Gonzalez, T.2    Le Marchand-Brustel, Y.3    Tanti, J.F.4
  • 142
    • 0026559095 scopus 로고
    • Caveolin, a protein component of caveolae membrane coats
    • 1739974 1:CAS:528:DyaK38XhvFWnurY%3D 10.1016/0092-8674(92)90143-Z
    • Rothberg KG, Heuser JE, Donzell WC, Ying YS, Glenney JR, et al. (1992) Caveolin, a protein component of caveolae membrane coats. Cell 68:673-682
    • (1992) Cell , vol.68 , pp. 673-682
    • Rothberg, K.G.1    Heuser, J.E.2    Donzell, W.C.3    Ying, Y.S.4    Glenney, J.R.5
  • 143
    • 0028027709 scopus 로고
    • Induction of caveolin during adipogenesis and association of GLUT4 with caveolin-rich vesicles
    • 7962086 1:CAS:528:DyaK2cXmslOnu7w%3D 10.1083/jcb.127.5.1233
    • Scherer PE, Lisanti MP, Baldini G, Sargiacomo M, Mastick CC, et al. (1994) Induction of caveolin during adipogenesis and association of GLUT4 with caveolin-rich vesicles. J Cell Biol 127:1233-1243
    • (1994) J Cell Biol , vol.127 , pp. 1233-1243
    • Scherer, P.E.1    Lisanti, M.P.2    Baldini, G.3    Sargiacomo, M.4    Mastick, C.C.5
  • 144
    • 0030744872 scopus 로고    scopus 로고
    • Insulin-stimulated tyrosine phosphorylation of caveolin is specific for the differentiated adipocyte phenotype in 3T3-L1 cells
    • 9252391 1:CAS:528:DyaK2sXlsFKrs78%3D 10.1074/jbc.272.33.20706
    • Mastick CC, Saltiel AR (1997) Insulin-stimulated tyrosine phosphorylation of caveolin is specific for the differentiated adipocyte phenotype in 3T3-L1 cells. J Biol Chem 272:20706-20714
    • (1997) J Biol Chem , vol.272 , pp. 20706-20714
    • Mastick, C.C.1    Saltiel, A.R.2
  • 145
    • 0029019438 scopus 로고
    • Insulin stimulates the tyrosine phosphorylation of caveolin
    • 7540611 1:CAS:528:DyaK2MXmt1antrw%3D 10.1083/jcb.129.6.1523
    • Mastick CC, Brady MJ, Saltiel AR (1995) Insulin stimulates the tyrosine phosphorylation of caveolin. J Cell Biol 129:1523-1531
    • (1995) J Cell Biol , vol.129 , pp. 1523-1531
    • Mastick, C.C.1    Brady, M.J.2    Saltiel, A.R.3
  • 146
    • 0037119387 scopus 로고    scopus 로고
    • The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1
    • 12036959 1:CAS:528:DC%2BD38XmsVKhsb8%3D 10.1074/jbc.M203375200
    • Kimura A, Mora S, Shigematsu S, Pessin JE, Saltiel AR (2002) The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1. J Biol Chem 277:30153-30158
    • (2002) J Biol Chem , vol.277 , pp. 30153-30158
    • Kimura, A.1    Mora, S.2    Shigematsu, S.3    Pessin, J.E.4    Saltiel, A.R.5
  • 147
    • 0037663884 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue
    • 12660144 1:CAS:528:DC%2BD3sXls1Wntbs%3D 10.1152/ajpcell.00006.2003
    • Cohen AW, Razani B, Wang XB, Combs TP, Williams TM, et al. (2003) Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue. Am J Physiol Cell Physiol 285:C222-C235
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Cohen, A.W.1    Razani, B.2    Wang, X.B.3    Combs, T.P.4    Williams, T.M.5
  • 148
    • 0030060941 scopus 로고    scopus 로고
    • Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle
    • 8567687 1:CAS:528:DyaK28Xns1SjtQ%3D%3D 10.1074/jbc.271.4.2255
    • Tang Z, Scherer PE, Okamoto T, Song K, Chu C, et al. (1996) Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J Biol Chem 271:2255-2261
    • (1996) J Biol Chem , vol.271 , pp. 2255-2261
    • Tang, Z.1    Scherer, P.E.2    Okamoto, T.3    Song, K.4    Chu, C.5
  • 149
    • 4344701192 scopus 로고    scopus 로고
    • Insulin resistance in skeletal muscles of caveolin-3-null mice
    • 15314230 10.1073/pnas.0402053101
    • Oshikawa J, Otsu K, Toya Y, Tsunematsu T, Hankins R, et al. (2004) Insulin resistance in skeletal muscles of caveolin-3-null mice. Proc Natl Acad Sci USA 101:12670-12675
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12670-12675
    • Oshikawa, J.1    Otsu, K.2    Toya, Y.3    Tsunematsu, T.4    Hankins, R.5
  • 150
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities
    • 11259414 1:CAS:528:DC%2BD3MXksFGlurw%3D 10.1074/jbc.M100828200
    • Galbiati F, Engelman JA, Volonte D, Zhang XL, Minetti C, et al. (2001) Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities. J Biol Chem 276:21425-21433
    • (2001) J Biol Chem , vol.276 , pp. 21425-21433
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5
  • 151
    • 33646258495 scopus 로고    scopus 로고
    • Spatial and temporal regulation of GLUT4 translocation by flotillin-1 and caveolin-3 in skeletal muscle cells
    • 16455755 1:CAS:528:DC%2BD28XjtlGrtLs%3D
    • Fecchi K, Volonte D, Hezel MP, Schmeck K, Galbiati F (2006) Spatial and temporal regulation of GLUT4 translocation by flotillin-1 and caveolin-3 in skeletal muscle cells. FASEB J 20:705-707
    • (2006) FASEB J , vol.20 , pp. 705-707
    • Fecchi, K.1    Volonte, D.2    Hezel, M.P.3    Schmeck, K.4    Galbiati, F.5
  • 152
    • 0030969764 scopus 로고    scopus 로고
    • Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4
    • 9045631 1:CAS:528:DyaK2sXhvVOrtL4%3D 10.1074/jbc.272.10.6179
    • Tellam JT, Macaulay SL, McIntosh S, Hewish DR, Ward CW, et al. (1997) Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. J Biol Chem 272:6179-6186
    • (1997) J Biol Chem , vol.272 , pp. 6179-6186
    • Tellam, J.T.1    Macaulay, S.L.2    McIntosh, S.3    Hewish, D.R.4    Ward, C.W.5
  • 153
    • 0032509214 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated GLUT4 translocation by munc18c in 3T3L1 adipocytes
    • 9837979 1:CAS:528:DyaK1MXlsFU%3D 10.1074/jbc.273.50.33876
    • Thurmond DC, Ceresa BP, Okada S, Elmendorf JS, Coker K, et al. (1998) Regulation of insulin-stimulated GLUT4 translocation by munc18c in 3T3L1 adipocytes. J Biol Chem 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
  • 154
    • 37549069753 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Munc18c regulates platelet-derived growth factor-stimulated glucose transporter 4 translocation in 3T3L1 adipocytes
    • 17916632 1:CAS:528:DC%2BD1cXjtVyjsA%3D%3D 10.1210/en.2006-1549 (Epub 2007 Oct 2004)
    • Umahara M, Okada S, Yamada E, Saito T, Ohshima K, et al. (2008) Tyrosine phosphorylation of Munc18c regulates platelet-derived growth factor-stimulated glucose transporter 4 translocation in 3T3L1 adipocytes. Endocrinology 149:40-49 (Epub 2007 Oct 2004)
    • (2008) Endocrinology , vol.149 , pp. 40-49
    • Umahara, M.1    Okada, S.2    Yamada, E.3    Saito, T.4    Ohshima, K.5
  • 155
    • 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
    • 7513704 1:CAS:528:DyaK2cXjtFKgsrY%3D
    • Sasaoka T, Rose DW, Jhun BH, Saltiel AR, Draznin B, et al. (1994) 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 269:13689-13694
    • (1994) J Biol Chem , vol.269 , pp. 13689-13694
    • Sasaoka, T.1    Rose, D.W.2    Jhun, B.H.3    Saltiel, A.R.4    Draznin, B.5
  • 156
    • 0042570843 scopus 로고    scopus 로고
    • Protein-protein interaction in insulin signaling and the molecular mechanisms of insulin resistance
    • 10194465 1:CAS:528:DyaK1MXitlegs78%3D 10.1172/JCI6609
    • Virkamaki A, Ueki K, Kahn CR (1999) Protein-protein interaction in insulin signaling and the molecular mechanisms of insulin resistance. J Clin Invest 103:931-943
    • (1999) J Clin Invest , vol.103 , pp. 931-943
    • Virkamaki, A.1    Ueki, K.2    Kahn, C.R.3
  • 157
    • 0344855590 scopus 로고    scopus 로고
    • Insulin-induced tyrosine phosphorylation of Shc in liver, muscle and adipose tissue of insulin resistant rats
    • 10612430 1:CAS:528:DyaK1MXmsFaitLY%3D 10.1016/S0303-7207(99)00137-9
    • Paez-Espinosa EV, Rocha EM, Velloso LA, Boschero AC, Saad MJ (1999) Insulin-induced tyrosine phosphorylation of Shc in liver, muscle and adipose tissue of insulin resistant rats. Mol Cell Endocrinol 156:121-129
    • (1999) Mol Cell Endocrinol , vol.156 , pp. 121-129
    • Paez-Espinosa, E.V.1    Rocha, E.M.2    Velloso, L.A.3    Boschero, A.C.4    Saad, M.J.5
  • 158
    • 13344278677 scopus 로고    scopus 로고
    • Interaction between the phosphotyrosine binding domain of Shc and the insulin receptor is required for Shc phosphorylation by insulin in vivo
    • 8626723 1:CAS:528:DyaK28XhtlSmsr8%3D 10.1074/jbc.271.8.3959
    • Isakoff SJ, Yu YP, Su YC, Blaikie P, Yajnik V, et al. (1996) Interaction between the phosphotyrosine binding domain of Shc and the insulin receptor is required for Shc phosphorylation by insulin in vivo. J Biol Chem 271:3959-3962
    • (1996) J Biol Chem , vol.271 , pp. 3959-3962
    • Isakoff, S.J.1    Yu, Y.P.2    Su, Y.C.3    Blaikie, P.4    Yajnik, V.5
  • 159
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain
    • 7537849 1:STN:280:DyaK2M3lsl2gsw%3D%3D
    • Gustafson TA, He W, Craparo A, Schaub CD, O'Neill TJ (1995) Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol Cell Biol 15:2500-2508
    • (1995) Mol Cell Biol , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 160
    • 0028783488 scopus 로고
    • Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via Non-SH2 domains
    • 7559478 1:CAS:528:DyaK2MXos1eit7c%3D 10.1074/jbc.270.40.23258
    • He W, O'Neill T, Gustafson T (1995) Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via Non-SH2 domains. J Biol Chem 270:23258-23262
    • (1995) J Biol Chem , vol.270 , pp. 23258-23262
    • He, W.1    O'Neill, T.2    Gustafson, T.3
  • 161
    • 0029830017 scopus 로고    scopus 로고
    • Functional importance of amino-terminal domain of Shc for interaction with insulin and epidermal growth factor receptors in phosphorylation- independent manner
    • 8702728 1:CAS:528:DyaK28XltVKrtrs%3D 10.1074/jbc.271.33.20082
    • Sasaoka T, Ishihara H, Sawa T, Ishiki M, Morioka H, et al. (1996) Functional importance of amino-terminal domain of Shc for interaction with insulin and epidermal growth factor receptors in phosphorylation-independent manner. J Biol Chem 271:20082-20087
    • (1996) J Biol Chem , vol.271 , pp. 20082-20087
    • Sasaoka, T.1    Ishihara, H.2    Sawa, T.3    Ishiki, M.4    Morioka, H.5
  • 162
    • 0027288587 scopus 로고
    • The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS-1 and Shc: Implications for insulin control of ras signalling
    • 8491186 1:CAS:528:DyaK3sXksVWnsr8%3D
    • Skolnik E, Lee C, Batzer A, Vicentini L, Zhou M, et al. (1993) The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS-1 and Shc: implications for insulin control of ras signalling. EMBO J 12:1929-1936
    • (1993) EMBO J , vol.12 , pp. 1929-1936
    • Skolnik, E.1    Lee, C.2    Batzer, A.3    Vicentini, L.4    Zhou, M.5
  • 163
    • 0028341446 scopus 로고
    • Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation
    • 8144662 1:CAS:528:DyaK2cXis1WrtL4%3D
    • Sasaoka T, Draznin B, Leitner JW, Langlois WJ, Olefsky JM (1994) Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation. J Biol Chem 269:10734-10738
    • (1994) J Biol Chem , vol.269 , pp. 10734-10738
    • Sasaoka, T.1    Draznin, B.2    Leitner, J.W.3    Langlois, W.J.4    Olefsky, J.M.5
  • 164
    • 0028036724 scopus 로고
    • Insulin receptor substrate-1 (IRS1) and Shc compete for a limited pool of Grb2 in mediating insulin downstream signaling
    • 7983051 1:CAS:528:DyaK2cXmslalsLw%3D
    • Yamauchi K, Pessin JE (1994) Insulin receptor substrate-1 (IRS1) and Shc compete for a limited pool of Grb2 in mediating insulin downstream signaling. J Biol Chem 269:31107-31114
    • (1994) J Biol Chem , vol.269 , pp. 31107-31114
    • Yamauchi, K.1    Pessin, J.E.2
  • 165
    • 0030028790 scopus 로고    scopus 로고
    • A Grb2-associated docking protein in EGF-and insulin-receptor signalling
    • 8596638 1:CAS:528:DyaK28XhtVWhtr8%3D 10.1038/379560a0
    • Holgado-Madruga M, Emlet DR, Moscatello DK, Godwin AK, Wong AJ (1996) A Grb2-associated docking protein in EGF-and insulin-receptor signalling. Nature 379:560-564
    • (1996) Nature , vol.379 , pp. 560-564
    • Holgado-Madruga, M.1    Emlet, D.R.2    Moscatello, D.K.3    Godwin, A.K.4    Wong, A.J.5
  • 166
    • 40649117198 scopus 로고    scopus 로고
    • Dissection of the insulin signaling pathway via quantitative phosphoproteomics
    • 18268350 10.1073/pnas.0711713105
    • Kruger M, Kratchmarova I, Blagoev B, Tseng YH, Kahn CR, et al. (2008) Dissection of the insulin signaling pathway via quantitative phosphoproteomics. Proc Natl Acad Sci USA 105:2451-2456
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 2451-2456
    • Kruger, M.1    Kratchmarova, I.2    Blagoev, B.3    Tseng, Y.H.4    Kahn, C.R.5
  • 167
    • 1942501808 scopus 로고    scopus 로고
    • A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C] tyrosine
    • 14739304 1:CAS:528:DC%2BD2cXivF2rurs%3D 10.1074/jbc.M311714200
    • Ibarrola N, Molina H, Iwahori A, Pandey A (2004) A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C] tyrosine. J Biol Chem 279:15805-15813
    • (2004) J Biol Chem , vol.279 , pp. 15805-15813
    • Ibarrola, N.1    Molina, H.2    Iwahori, A.3    Pandey, A.4
  • 168
    • 0032230233 scopus 로고    scopus 로고
    • Determination of Gab1 (Grb2-associated binder-1) interaction with insulin receptor-signaling molecules
    • 9658397 1:CAS:528:DyaK1cXktlOis7Y%3D 10.1210/me.12.7.914
    • Rocchi S, Tartare-Deckert S, Murdaca J, Holgado-Madruga M, Wong AJ, et al. (1998) Determination of Gab1 (Grb2-associated binder-1) interaction with insulin receptor-signaling molecules. Mol Endocrinol 12:914-923
    • (1998) Mol Endocrinol , vol.12 , pp. 914-923
    • Rocchi, S.1    Tartare-Deckert, S.2    Murdaca, J.3    Holgado-Madruga, M.4    Wong, A.J.5
  • 169
    • 0031452395 scopus 로고    scopus 로고
    • Identification of Stat 5B as a substrate of the insulin receptor
    • 9428692 1:CAS:528:DyaK1cXjsFamug%3D%3D 10.1111/j.1432-1033.1997.0411a.x
    • Sawka-Verhelle D, Filloux C, Tartare-Deckert S, Mothe I, Van Obberghen E (1997) Identification of Stat 5B as a substrate of the insulin receptor. Eur J Biochem 250:411-417
    • (1997) Eur J Biochem , vol.250 , pp. 411-417
    • Sawka-Verhelle, D.1    Filloux, C.2    Tartare-Deckert, S.3    Mothe, I.4    Van Obberghen, E.5
  • 170
    • 0030900715 scopus 로고    scopus 로고
    • Stat5 is a physiological substrate of the insulin receptor
    • 9122188 1:CAS:528:DyaK2sXhvF2ltbY%3D 10.1073/pnas.94.6.2295
    • Chen J, Sadowski HB, Kohanski RA, Wang LH (1997) Stat5 is a physiological substrate of the insulin receptor. Proc Natl Acad Sci USA 94:2295-2300
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2295-2300
    • Chen, J.1    Sadowski, H.B.2    Kohanski, R.A.3    Wang, L.H.4
  • 171
    • 0035827663 scopus 로고    scopus 로고
    • Insulin Induction of SOCS-2 and SOCS-3 mRNA expression in C2C12 skeletal muscle cells is mediated by Stat5
    • 11279166 1:CAS:528:DC%2BD3MXktlKnu7k%3D 10.1074/jbc.M101014200
    • Sadowski CL, Choi TS, Le M, Wheeler TT, Wang LH, et al. (2001) Insulin Induction of SOCS-2 and SOCS-3 mRNA expression in C2C12 skeletal muscle cells is mediated by Stat5. J Biol Chem 276:20703-20710
    • (2001) J Biol Chem , vol.276 , pp. 20703-20710
    • Sadowski, C.L.1    Choi, T.S.2    Le, M.3    Wheeler, T.T.4    Wang, L.H.5
  • 172
    • 0030046753 scopus 로고    scopus 로고
    • STATs: Signal transducers and activators of transcription
    • 8608586 1:CAS:528:DyaK28XhtFWqsbY%3D 10.1016/S0092-8674(00)81277-5
    • Ihle JN (1996) STATs: signal transducers and activators of transcription. Cell 84:331-334
    • (1996) Cell , vol.84 , pp. 331-334
    • Ihle, J.N.1
  • 173
    • 0034458143 scopus 로고    scopus 로고
    • Stat 5B, activated by insulin in a Jak-independent fashion, plays a role in glucokinase gene transcription
    • 10830280 1:CAS:528:DC%2BD3cXlt1Wnu7s%3D 10.1210/en.141.6.1977
    • Sawka-Verhelle D, Tartare-Deckert S, Decaux JF, Girard J, Van Obberghen E (2000) Stat 5B, activated by insulin in a Jak-independent fashion, plays a role in glucokinase gene transcription. Endocrinology 141:1977-1988
    • (2000) Endocrinology , vol.141 , pp. 1977-1988
    • Sawka-Verhelle, D.1    Tartare-Deckert, S.2    Decaux, J.F.3    Girard, J.4    Van Obberghen, E.5
  • 174
    • 85047685503 scopus 로고    scopus 로고
    • Stimulation of 3T3-L1 adipogenesis by signal transducer and activator of transcription 5
    • 12089351 1:CAS:528:DC%2BD38XlsVGitbc%3D 10.1210/me.16.7.1565
    • Nanbu-Wakao R, Morikawa Y, Matsumura I, Masuho Y, Muramatsu MA, et al. (2002) Stimulation of 3T3-L1 adipogenesis by signal transducer and activator of transcription 5. Mol Endocrinol 16:1565-1576
    • (2002) Mol Endocrinol , vol.16 , pp. 1565-1576
    • Nanbu-Wakao, R.1    Morikawa, Y.2    Matsumura, I.3    Masuho, Y.4    Muramatsu, M.A.5
  • 175
    • 0030833570 scopus 로고    scopus 로고
    • Requirement of STAT5b for sexual dimorphism of body growth rates and liver gene expression
    • 9207075 1:CAS:528:DyaK2sXksFOgu7w%3D 10.1073/pnas.94.14.7239
    • Udy GB, Towers RP, Snell RG, Wilkins RJ, Park SH, et al. (1997) Requirement of STAT5b for sexual dimorphism of body growth rates and liver gene expression. Proc Natl Acad Sci USA 94:7239-7244
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7239-7244
    • Udy, G.B.1    Towers, R.P.2    Snell, R.G.3    Wilkins, R.J.4    Park, S.H.5
  • 176
    • 0034717062 scopus 로고    scopus 로고
    • SOCS-3 is an insulin-induced negative regulator of insulin signaling
    • 10821852 1:CAS:528:DC%2BD3cXjvFaisbo%3D 10.1074/jbc.275.21.15985
    • Emanuelli B, Peraldi P, Filloux C, Sawka-Verhelle D, Hilton D, et al. (2000) SOCS-3 is an insulin-induced negative regulator of insulin signaling. J Biol Chem 275:15985-15991
    • (2000) J Biol Chem , vol.275 , pp. 15985-15991
    • Emanuelli, B.1    Peraldi, P.2    Filloux, C.3    Sawka-Verhelle, D.4    Hilton, D.5
  • 177
    • 4143051437 scopus 로고    scopus 로고
    • WY-14643 and 9-cis-retinoic acid induce IRS-2/PI 3-kinase signalling pathway and increase glucose transport in human skeletal muscle cells: Differential effect in myotubes from healthy subjects and type 2 diabetic patients
    • 15292987 1:CAS:528:DC%2BD2cXmt1Kkt78%3D 10.1007/s00125-004-1428-1
    • Bouzakri K, Roques M, Debard C, Berbe V, Rieusset J, et al. (2004) WY-14643 and 9-cis-retinoic acid induce IRS-2/PI 3-kinase signalling pathway and increase glucose transport in human skeletal muscle cells: differential effect in myotubes from healthy subjects and type 2 diabetic patients. Diabetologia 47:1314-1323
    • (2004) Diabetologia , vol.47 , pp. 1314-1323
    • Bouzakri, K.1    Roques, M.2    Debard, C.3    Berbe, V.4    Rieusset, J.5
  • 178
    • 0028244396 scopus 로고
    • Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells
    • 8022486 1:CAS:528:DyaK2cXmslymsrc%3D 10.1038/370153a0
    • Witthuhn BA, Silvennoinen O, Miura O, Lai KS, Cwik C, et al. (1994) Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells. Nature 370:153-157
    • (1994) Nature , vol.370 , pp. 153-157
    • Witthuhn, B.A.1    Silvennoinen, O.2    Miura, O.3    Lai, K.S.4    Cwik, C.5
  • 179
    • 0026081302 scopus 로고
    • Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase
    • 1848670 1:CAS:528:DyaK3MXlslyju7s%3D
    • Wilks AF, Harpur AG, Kurban RR, Ralph SJ, Zurcher G, et al. (1991) Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. Mol Cell Biol 11:2057-2065
    • (1991) Mol Cell Biol , vol.11 , pp. 2057-2065
    • Wilks, A.F.1    Harpur, A.G.2    Kurban, R.R.3    Ralph, S.J.4    Zurcher, G.5
  • 180
    • 0024989359 scopus 로고
    • Tyk2, prototype of a novel class of non-receptor tyrosine kinase genes
    • 2216457 1:CAS:528:DyaK3MXhsFyjuro%3D
    • Firmbach-Kraft I, Byers M, Shows T, Dalla-Favera R, Krolewski JJ (1990) tyk2, prototype of a novel class of non-receptor tyrosine kinase genes. Oncogene 5:1329-1336
    • (1990) Oncogene , vol.5 , pp. 1329-1336
    • Firmbach-Kraft, I.1    Byers, M.2    Shows, T.3    Dalla-Favera, R.4    Krolewski, J.J.5
  • 181
    • 0026735084 scopus 로고
    • JAK2, a third member of the JAK family of protein tyrosine kinases
    • 1620548 1:CAS:528:DyaK38XmtVOrtLc%3D
    • Harpur AG, Andres AC, Ziemiecki A, Aston RR, Wilks AF (1992) JAK2, a third member of the JAK family of protein tyrosine kinases. Oncogene 7:1347-1353
    • (1992) Oncogene , vol.7 , pp. 1347-1353
    • Harpur, A.G.1    Andres, A.C.2    Ziemiecki, A.3    Aston, R.R.4    Wilks, A.F.5
  • 182
    • 0028875977 scopus 로고
    • Involvement of Janus kinases in the insulin signaling pathway
    • 8536716 1:CAS:528:DyaK2MXhtVSktbfI 10.1111/j.1432-1033.1995.656-b.x
    • Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E (1995) Involvement of Janus kinases in the insulin signaling pathway. Eur J Biochem 234:656-660
    • (1995) Eur J Biochem , vol.234 , pp. 656-660
    • Giorgetti-Peraldi, S.1    Peyrade, F.2    Baron, V.3    Van Obberghen, E.4
  • 183
    • 0029786390 scopus 로고    scopus 로고
    • Insulin induces tyrosine phosphorylation of JAK2 in insulin-sensitive tissues of the intact rat
    • 8703019 1:CAS:528:DyaK28XlsFKntrY%3D 10.1074/jbc.271.36.22100
    • Saad MJ, Carvalho CR, Thirone AC, Velloso LA (1996) Insulin induces tyrosine phosphorylation of JAK2 in insulin-sensitive tissues of the intact rat. J Biol Chem 271:22100-22104
    • (1996) J Biol Chem , vol.271 , pp. 22100-22104
    • Saad, M.J.1    Carvalho, C.R.2    Thirone, A.C.3    Velloso, L.A.4
  • 184
    • 0031769049 scopus 로고    scopus 로고
    • Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor
    • 9492017 1:CAS:528:DyaK1cXhtlejsbk%3D 10.1210/en.139.3.884
    • Gual P, Baron V, Lequoy V, Van Obberghen E (1998) Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor. Endocrinology 139:884-893
    • (1998) Endocrinology , vol.139 , pp. 884-893
    • Gual, P.1    Baron, V.2    Lequoy, V.3    Van Obberghen, E.4
  • 185
    • 0025676428 scopus 로고
    • Insulin receptor tyrosine kinase-catalyzed phosphorylation of 422(aP2) protein. Substrate activation by long-chain fatty acid
    • 2174434 1:CAS:528:DyaK3cXmtVOgsLs%3D
    • Hresko RC, Hoffman RD, Flores-Riveros JR, Lane MD (1990) Insulin receptor tyrosine kinase-catalyzed phosphorylation of 422(aP2) protein. Substrate activation by long-chain fatty acid. J Biol Chem 265:21075-21085
    • (1990) J Biol Chem , vol.265 , pp. 21075-21085
    • Hresko, R.C.1    Hoffman, R.D.2    Flores-Riveros, J.R.3    Lane, M.D.4
  • 186
    • 0024269622 scopus 로고
    • Identification of phosphorylated 422 (aP2) protein as pp 15, the 15-kilodalton target of the insulin receptor tyrosine kinase in 3T3-L1 adipocytes
    • 2848242 1:CAS:528:DyaL1MXntFKrtw%3D%3D 10.1073/pnas.85.23.8835
    • Hresko RC, Bernier M, Hoffman RD, Flores-Riveros JR, Liao K, et al. (1988) Identification of phosphorylated 422 (aP2) protein as pp 15, the 15-kilodalton target of the insulin receptor tyrosine kinase in 3T3-L1 adipocytes. Proc Natl Acad Sci USA 85:8835-8839
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8835-8839
    • Hresko, R.C.1    Bernier, M.2    Hoffman, R.D.3    Flores-Riveros, J.R.4    Liao, K.5
  • 187
    • 0027502045 scopus 로고
    • Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity
    • 8452530 1:CAS:528:DyaK3sXhvVeqtLw%3D
    • Soos MA, Field CE, Siddle K (1993) Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity. Biochem J 290:419-426
    • (1993) Biochem J , vol.290 , pp. 419-426
    • Soos, M.A.1    Field, C.E.2    Siddle, K.3
  • 188
    • 0032800850 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor-I (IGF-I) receptor overexpression in breast cancers leads to insulin/IGF-I hybrid receptor overexpression: Evidence for a second mechanism of IGF-I signaling
    • 10430101 1:CAS:528:DyaK1MXltVCqtL8%3D
    • Pandini G, Vigneri R, Costantino A, Frasca F, Ippolito A, et al. (1999) Insulin and insulin-like growth factor-I (IGF-I) receptor overexpression in breast cancers leads to insulin/IGF-I hybrid receptor overexpression: evidence for a second mechanism of IGF-I signaling. Clin Cancer Res 5:1935-1944
    • (1999) Clin Cancer Res , vol.5 , pp. 1935-1944
    • Pandini, G.1    Vigneri, R.2    Costantino, A.3    Frasca, F.4    Ippolito, A.5
  • 189
    • 0029095525 scopus 로고
    • The B isoform of the insulin receptor signals more efficiently than the A isoform in HepG2 cells
    • 7657666 1:CAS:528:DyaK2MXnvVOqu7g%3D 10.1074/jbc.270.35.20816
    • Kosaki A, Pillay TS, Xu L, Webster NJ (1995) The B isoform of the insulin receptor signals more efficiently than the A isoform in HepG2 cells. J Biol Chem 270:20816-20823
    • (1995) J Biol Chem , vol.270 , pp. 20816-20823
    • Kosaki, A.1    Pillay, T.S.2    Xu, L.3    Webster, N.J.4
  • 190
    • 0032709249 scopus 로고    scopus 로고
    • Insulin/IGF-I hybrid receptors play a major role in IGF-I signaling in thyroid cancer
    • 10401676 1:CAS:528:DyaK1MXktVSis7k%3D 10.1016/S0300-9084(99)80088-1
    • Belfiore A, Pandini G, Vella V, Squatrito S, Vigneri R (1999) Insulin/IGF-I hybrid receptors play a major role in IGF-I signaling in thyroid cancer. Biochimie 81:403-407
    • (1999) Biochimie , vol.81 , pp. 403-407
    • Belfiore, A.1    Pandini, G.2    Vella, V.3    Squatrito, S.4    Vigneri, R.5
  • 191
    • 34047174592 scopus 로고    scopus 로고
    • The role of insulin receptor isoforms and hybrid insulin/IGF-I receptors in human cancer
    • 17346183 1:CAS:528:DC%2BD2sXlsVagtr8%3D 10.2174/138161207780249173
    • Belfiore A (2007) The role of insulin receptor isoforms and hybrid insulin/IGF-I receptors in human cancer. Curr Pharm Des 13:671-686
    • (2007) Curr Pharm des , vol.13 , pp. 671-686
    • Belfiore, A.1
  • 192
    • 14844293962 scopus 로고    scopus 로고
    • The role of insulin and IGF-1 signaling in longevity
    • 15723168 1:CAS:528:DC%2BD2MXktlantrk%3D 10.1007/s00018-004-4297-y
    • Katic M, Kahn CR (2005) The role of insulin and IGF-1 signaling in longevity. Cell Mol Life Sci 62:320-343
    • (2005) Cell Mol Life Sci , vol.62 , pp. 320-343
    • Katic, M.1    Kahn, C.R.2
  • 193
    • 34548190256 scopus 로고    scopus 로고
    • Endocrine regulation of ageing
    • 17684529 1:CAS:528:DC%2BD2sXpsVartLk%3D 10.1038/nrm2234
    • Russell SJ, Kahn CR (2007) Endocrine regulation of ageing. Nat Rev Mol Cell Biol 8:681-691
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 681-691
    • Russell, S.J.1    Kahn, C.R.2
  • 194
    • 27544434895 scopus 로고    scopus 로고
    • The insulin/IGF-1 signaling in mammals and its relevance to human longevity
    • 16168602 1:CAS:528:DC%2BD2MXhtFyksLnP 10.1016/j.exger.2005.06.014
    • Rincon M, Rudin E, Barzilai N (2005) The insulin/IGF-1 signaling in mammals and its relevance to human longevity. Exp Gerontol 40:873-877
    • (2005) Exp Gerontol , vol.40 , pp. 873-877
    • Rincon, M.1    Rudin, E.2    Barzilai, N.3
  • 195
    • 2942536602 scopus 로고    scopus 로고
    • The paradox of the insulin/IGF-1 signaling pathway in longevity
    • 15272501 1:CAS:528:DC%2BD2cXks1Wksbs%3D 10.1016/j.mad.2004.03.006
    • Rincon M, Muzumdar R, Atzmon G, Barzilai N (2004) The paradox of the insulin/IGF-1 signaling pathway in longevity. Mech Ageing Dev 125:397-403
    • (2004) Mech Ageing Dev , vol.125 , pp. 397-403
    • Rincon, M.1    Muzumdar, R.2    Atzmon, G.3    Barzilai, N.4
  • 196
    • 0035815445 scopus 로고    scopus 로고
    • A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function
    • 11292875 1:CAS:528:DC%2BD3MXis1Grt74%3D 10.1126/science.1057987
    • Tatar M, Kopelman A, Epstein D, Tu MP, Yin CM, et al. (2001) A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function. Science 292:107-110
    • (2001) Science , vol.292 , pp. 107-110
    • Tatar, M.1    Kopelman, A.2    Epstein, D.3    Tu, M.P.4    Yin, C.M.5
  • 197
    • 0035815414 scopus 로고    scopus 로고
    • Extension of life-span by loss of CHICO, a Drosophila insulin receptor substrate protein
    • 11292874 1:CAS:528:DC%2BD3MXis1Grtrc%3D 10.1126/science.1057991
    • Clancy DJ, Gems D, Harshman LG, Oldham S, Stocker H, et al. (2001) Extension of life-span by loss of CHICO, a Drosophila insulin receptor substrate protein. Science 292:104-106
    • (2001) Science , vol.292 , pp. 104-106
    • Clancy, D.J.1    Gems, D.2    Harshman, L.G.3    Oldham, S.4    Stocker, H.5
  • 198
    • 0027771804 scopus 로고
    • AC elegans mutant that lives twice as long as wild type
    • 8247153 1:STN:280:DyaK2c%2FmslensQ%3D%3D 10.1038/366461a0
    • Kenyon C, Chang J, Gensch E, Rudner A, Tabtiang R (1993) A C. elegans mutant that lives twice as long as wild type. Nature 366:461-464
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 199
    • 0030813398 scopus 로고    scopus 로고
    • Daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans
    • 9252323 1:CAS:528:DyaK2sXltlCqsb0%3D 10.1126/science.277.5328.942
    • Kimura KD, Tissenbaum HA, Liu Y, Ruvkun G (1997) daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans. Science 277:942-946
    • (1997) Science , vol.277 , pp. 942-946
    • Kimura, K.D.1    Tissenbaum, H.A.2    Liu, Y.3    Ruvkun, G.4
  • 200
    • 55849101681 scopus 로고    scopus 로고
    • Fat metabolism links germline stem cells and longevity in C. Elegans
    • 18988854 1:CAS:528:DC%2BD1cXhtlaltLzI 10.1126/science.1162011
    • Wang MC, O'Rourke EJ, Ruvkun G (2008) Fat metabolism links germline stem cells and longevity in C. elegans. Science 322:957-960
    • (2008) Science , vol.322 , pp. 957-960
    • Wang, M.C.1    O'Rourke, E.J.2    Ruvkun, G.3
  • 201
    • 0037448528 scopus 로고    scopus 로고
    • Genome-wide RNAi analysis of Caenorhabditis elegans fat regulatory genes
    • 12529643 1:CAS:528:DC%2BD3sXjsF2htw%3D%3D 10.1038/nature01279
    • Ashrafi K, Chang FY, Watts JL, Fraser AG, Kamath RS, et al. (2003) Genome-wide RNAi analysis of Caenorhabditis elegans fat regulatory genes. Nature 421:268-272
    • (2003) Nature , vol.421 , pp. 268-272
    • Ashrafi, K.1    Chang, F.Y.2    Watts, J.L.3    Fraser, A.G.4    Kamath, R.S.5
  • 202
    • 0033636523 scopus 로고    scopus 로고
    • Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction
    • 10949030 1:CAS:528:DC%2BD3cXls1Kls7g%3D
    • Michael MD, Kulkarni RN, Postic C, Previs SF, Shulman GI, et al. (2000) Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction. Mol Cell 6:87-97
    • (2000) Mol Cell , vol.6 , pp. 87-97
    • Michael, M.D.1    Kulkarni, R.N.2    Postic, C.3    Previs, S.F.4    Shulman, G.I.5
  • 203
    • 0033524937 scopus 로고    scopus 로고
    • Tissue-specific knockout of the insulin receptor in pancreatic beta cells creates an insulin secretory defect similar to that in type 2 diabetes
    • 10025399 1:CAS:528:DyaK1MXht1eqsrc%3D 10.1016/S0092-8674(00)80546-2
    • Kulkarni RN, Bruning JC, Winnay JN, Postic C, Magnuson MA, et al. (1999) Tissue-specific knockout of the insulin receptor in pancreatic beta cells creates an insulin secretory defect similar to that in type 2 diabetes. Cell 96:329-339
    • (1999) Cell , vol.96 , pp. 329-339
    • Kulkarni, R.N.1    Bruning, J.C.2    Winnay, J.N.3    Postic, C.4    Magnuson, M.A.5
  • 204
    • 0034703229 scopus 로고    scopus 로고
    • Role of brain insulin receptor in control of body weight and reproduction
    • 11000114 1:CAS:528:DC%2BD3cXmvVClsLY%3D 10.1126/science.289.5487.2122
    • Bruning JC, Gautam D, Burks DJ, Gillette J, Schubert M, et al. (2000) Role of brain insulin receptor in control of body weight and reproduction. Science 289:2122-2125
    • (2000) Science , vol.289 , pp. 2122-2125
    • Bruning, J.C.1    Gautam, D.2    Burks, D.J.3    Gillette, J.4    Schubert, M.5
  • 205
    • 0024160877 scopus 로고
    • Banting lecture 1988. Role of insulin resistance in human disease
    • 3056758 1:STN:280:DyaL1M%2Flt12msQ%3D%3D 10.2337/diabetes.37.12.1595
    • Reaven GM (1988) Banting lecture 1988. Role of insulin resistance in human disease. Diabetes 37:1595-1607
    • (1988) Diabetes , vol.37 , pp. 1595-1607
    • Reaven, G.M.1
  • 206
    • 77954629358 scopus 로고    scopus 로고
    • Fat tissue and long life
    • 20054178 10.1159/000145930
    • Bluher M (2008) Fat tissue and long life. Obes Facts 1:176-182
    • (2008) Obes Facts , vol.1 , pp. 176-182
    • Bluher, M.1
  • 207
    • 0034012605 scopus 로고    scopus 로고
    • Effects of glucose ingestion on cardiac autonomic nervous system in healthy centenarians: Differences with aged subjects
    • 10759874 1:CAS:528:DC%2BD3cXjsFCqsb8%3D 10.1046/j.1365-2362.2000.00626.x
    • Paolisso G, Manzella D, Rizzo MR, Barbieri M, Gambardella A, et al. (2000) Effects of glucose ingestion on cardiac autonomic nervous system in healthy centenarians: differences with aged subjects. Eur J Clin Invest 30:277-284
    • (2000) Eur J Clin Invest , vol.30 , pp. 277-284
    • Paolisso, G.1    Manzella, D.2    Rizzo, M.R.3    Barbieri, M.4    Gambardella, A.5
  • 208
    • 14844317297 scopus 로고    scopus 로고
    • Molecular links between aging and adipose tissue
    • 1:CAS:528:DC%2BD2MXht1Omt7c%3D 10.1038/sj.ijo.0802912
    • Picard F, Guarente L (2005) Molecular links between aging and adipose tissue. Int J Obes (Lond) 29(Suppl 1):S36-S39
    • (2005) Int J Obes (Lond) , vol.29 , Issue.SUPPL. 1
    • Picard, F.1    Guarente, L.2
  • 209
    • 40449142493 scopus 로고    scopus 로고
    • Evidence for lifespan extension and delayed age-related biomarkers in insulin receptor substrate 1 null mice
    • 17928362 1:CAS:528:DC%2BD1cXjtVaqsL0%3D 10.1096/fj.07-9261com
    • Selman C, Lingard S, Choudhury AI, Batterham RL, Claret M, et al. (2008) Evidence for lifespan extension and delayed age-related biomarkers in insulin receptor substrate 1 null mice. FASEB J 22:807-818
    • (2008) FASEB J , vol.22 , pp. 807-818
    • Selman, C.1    Lingard, S.2    Choudhury, A.I.3    Batterham, R.L.4    Claret, M.5
  • 210
    • 77950200010 scopus 로고    scopus 로고
    • The genetics of ageing
    • 20336132 1:CAS:528:DC%2BC3cXjvVGltLk%3D 10.1038/nature08980
    • Kenyon CJ (2010) The genetics of ageing. Nature 464:504-512
    • (2010) Nature , vol.464 , pp. 504-512
    • Kenyon, C.J.1
  • 211
    • 0033151613 scopus 로고    scopus 로고
    • A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans
    • 10364160 1:CAS:528:DyaK1MXjvVahsbw%3D 10.1101/gad.13.11.1438
    • Paradis S, Ailion M, Toker A, Thomas JH, Ruvkun G (1999) A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans. Genes Dev 13:1438-1452
    • (1999) Genes Dev , vol.13 , pp. 1438-1452
    • Paradis, S.1    Ailion, M.2    Toker, A.3    Thomas, J.H.4    Ruvkun, G.5
  • 212
    • 0030659557 scopus 로고    scopus 로고
    • The fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. Elegans
    • 9353126 1:CAS:528:DyaK2sXntVartrs%3D 10.1038/40194
    • Ogg S, Paradis S, Gottlieb S, Patterson GI, Lee L, et al. (1997) The fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans. Nature 389:994-999
    • (1997) Nature , vol.389 , pp. 994-999
    • Ogg, S.1    Paradis, S.2    Gottlieb, S.3    Patterson, G.I.4    Lee, L.5
  • 213
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • 10910062 1:CAS:528:DC%2BD3cXkvFChsL0%3D
    • Sekulic A, Hudson CC, Homme JL, Yin P, Otterness DM, et al. (2000) A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res 60:3504-3513
    • (2000) Cancer Res , vol.60 , pp. 3504-3513
    • Sekulic, A.1    Hudson, C.C.2    Homme, J.L.3    Yin, P.4    Otterness, D.M.5
  • 214
    • 2942563805 scopus 로고    scopus 로고
    • Drosophila dFOXO controls lifespan and regulates insulin signalling in brain and fat body
    • 15175753 1:CAS:528:DC%2BD2cXks1Cgt7g%3D 10.1038/nature02549
    • Hwangbo DS, Gershman B, Tu MP, Palmer M, Tatar M (2004) Drosophila dFOXO controls lifespan and regulates insulin signalling in brain and fat body. Nature 429:562-566
    • (2004) Nature , vol.429 , pp. 562-566
    • Hwangbo, D.S.1    Gershman, B.2    Tu, M.P.3    Palmer, M.4    Tatar, M.5
  • 215
    • 67651151249 scopus 로고    scopus 로고
    • Association of common genetic variation in the insulin/IGF1 signaling pathway with human longevity
    • 19489743 1:CAS:528:DC%2BD1MXhtVSjtbbP 10.1111/j.1474-9726.2009.00493.x
    • Pawlikowska L, Hu D, Huntsman S, Sung A, Chu C, et al. (2009) Association of common genetic variation in the insulin/IGF1 signaling pathway with human longevity. Aging Cell 8:460-472
    • (2009) Aging Cell , vol.8 , pp. 460-472
    • Pawlikowska, L.1    Hu, D.2    Huntsman, S.3    Sung, A.4    Chu, C.5
  • 216
    • 70350359126 scopus 로고    scopus 로고
    • Genetic association of FOXO1A and FOXO3A with longevity trait in Han Chinese populations
    • 19793722 1:CAS:528:DC%2BD1MXhsVGltbvM 10.1093/hmg/ddp459
    • Li Y, Wang WJ, Cao H, Lu J, Wu C, et al. (2009) Genetic association of FOXO1A and FOXO3A with longevity trait in Han Chinese populations. Hum Mol Genet 18:4897-4904
    • (2009) Hum Mol Genet , vol.18 , pp. 4897-4904
    • Li, Y.1    Wang, W.J.2    Cao, H.3    Lu, J.4    Wu, C.5
  • 217
    • 35748929967 scopus 로고    scopus 로고
    • Genetic correlates of longevity and selected age-related phenotypes: A genome-wide association study in the Framingham Study
    • 17903295 10.1186/1471-2350-8-S1-S13 1:CAS:528:DC%2BD1cXjsFelsL0%3D
    • Lunetta KL, D'Agostino RB Sr, Karasik D, Benjamin EJ, Guo CY, et al. (2007) Genetic correlates of longevity and selected age-related phenotypes: a genome-wide association study in the Framingham Study. BMC Med Genet 8(Suppl 1):S13
    • (2007) BMC Med Genet , vol.8 , Issue.SUPPL. 1 , pp. 13
    • Lunetta, K.L.1    D'Agostino, Sr.R.B.2    Karasik, D.3    Benjamin, E.J.4    Guo, C.Y.5
  • 218
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • 12939617 1:CAS:528:DC%2BD3sXntFCitr4%3D 10.1038/nature01960
    • Howitz KT, Bitterman KJ, Cohen HY, Lamming DW, Lavu S, et al. (2003) Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425:191-196
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3    Lamming, D.W.4    Lavu, S.5
  • 219
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • 10521401 1:CAS:528:DyaK1MXmvFOitbc%3D 10.1101/gad.13.19.2570
    • Kaeberlein M, McVey M, Guarente L (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev 13:2570-2580
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 220
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • 15520384 1:CAS:528:DC%2BD2cXhtVGis77E 10.1073/pnas.0404184101
    • Rogina B, Helfand SL (2004) Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc Natl Acad Sci USA 101:15998-16003
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 221
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • 11242085 1:CAS:528:DC%2BD3MXitVyqtbg%3D 10.1038/35065638
    • Tissenbaum HA, Guarente L (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410:227-230
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 222
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes
    • 15788402 1:CAS:528:DC%2BD2MXktlCls7g%3D 10.1074/jbc.M412357200
    • Frescas D, Valenti L, Accili D (2005) Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J Biol Chem 280:20589-20595
    • (2005) J Biol Chem , vol.280 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 223
    • 33744976074 scopus 로고    scopus 로고
    • C. Elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span
    • 16777605 1:CAS:528:DC%2BD28XmsVOms7Y%3D 10.1016/j.cell.2006.04.036
    • Berdichevsky A, Viswanathan M, Horvitz HR, Guarente L (2006) C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell 125:1165-1177
    • (2006) Cell , vol.125 , pp. 1165-1177
    • Berdichevsky, A.1    Viswanathan, M.2    Horvitz, H.R.3    Guarente, L.4
  • 224
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • 15744310 1:CAS:528:DC%2BD2MXhslClsb0%3D 10.1038/nature03354
    • Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434:113-118
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5
  • 225
    • 80555142897 scopus 로고    scopus 로고
    • Sirt1 enhances skeletal muscle insulin sensitivity in mice during caloric restriction
    • 21985785 1:CAS:528:DC%2BC3MXhsVCksLzP 10.1172/JCI58554
    • Schenk S, McCurdy CE, Philp A, Chen MZ, Holliday MJ, et al. (2011) Sirt1 enhances skeletal muscle insulin sensitivity in mice during caloric restriction. J Clin Invest 121:4281-4288
    • (2011) J Clin Invest , vol.121 , pp. 4281-4288
    • Schenk, S.1    McCurdy, C.E.2    Philp, A.3    Chen, M.Z.4    Holliday, M.J.5
  • 226
    • 48349144852 scopus 로고    scopus 로고
    • Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span
    • 18599363 1:CAS:528:DC%2BD1cXpvVKrs74%3D 10.1016/j.cmet.2008.06.011
    • Pearson KJ, Baur JA, Lewis KN, Peshkin L, Price NL, et al. (2008) Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span. Cell Metab 8:157-168
    • (2008) Cell Metab , vol.8 , pp. 157-168
    • Pearson, K.J.1    Baur, J.A.2    Lewis, K.N.3    Peshkin, L.4    Price, N.L.5
  • 227
    • 79951726016 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase as a novel functional target for the regulation of the insulin signaling pathway by SIRT1
    • 21241768 10.1016/j.mce.2011.01.008 1:CAS:528:DC%2BC3MXit1Ggs7o%3D
    • Frojdo S, Durand C, Molin L, Carey AL, El-Osta A, et al. (2011) Phosphoinositide 3-kinase as a novel functional target for the regulation of the insulin signaling pathway by SIRT1. Mol Cell Endocrinol 335:166-176
    • (2011) Mol Cell Endocrinol , vol.335 , pp. 166-176
    • Frojdo, S.1    Durand, C.2    Molin, L.3    Carey, A.L.4    El-Osta, A.5
  • 228
    • 61749095297 scopus 로고    scopus 로고
    • SIRT1 exerts anti-inflammatory effects and improves insulin sensitivity in adipocytes
    • 19103747 1:CAS:528:DC%2BD1MXitlylsrY%3D 10.1128/MCB.00705-08
    • Yoshizaki T, Milne JC, Imamura T, Schenk S, Sonoda N, et al. (2009) SIRT1 exerts anti-inflammatory effects and improves insulin sensitivity in adipocytes. Mol Cell Biol 29:1363-1374
    • (2009) Mol Cell Biol , vol.29 , pp. 1363-1374
    • Yoshizaki, T.1    Milne, J.C.2    Imamura, T.3    Schenk, S.4    Sonoda, N.5
  • 229
    • 14244256097 scopus 로고    scopus 로고
    • Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: Possible involvement in obesity-linked insulin resistance
    • 15604215 1:CAS:528:DC%2BD2MXitlehtb0%3D 10.1210/en.2004-0921
    • Khamzina L, Veilleux A, Bergeron S, Marette A (2005) Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance. Endocrinology 146:1473-1481
    • (2005) Endocrinology , vol.146 , pp. 1473-1481
    • Khamzina, L.1    Veilleux, A.2    Bergeron, S.3    Marette, A.4
  • 230
    • 0035851205 scopus 로고    scopus 로고
    • Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells
    • 11498541 1:CAS:528:DC%2BD3MXotFOrtbc%3D
    • Tremblay F, Marette A (2001) Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells. J Biol Chem 276:38052-38060
    • (2001) J Biol Chem , vol.276 , pp. 38052-38060
    • Tremblay, F.1    Marette, A.2
  • 231
    • 0034947869 scopus 로고    scopus 로고
    • Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin
    • 11438661 1:CAS:528:DC%2BD3MXlsVGitLw%3D 10.1128/MCB.21.15.5050-5062.2001
    • Takano A, Usui I, Haruta T, Kawahara J, Uno T, et al. (2001) Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin. Mol Cell Biol 21:5050-5062
    • (2001) Mol Cell Biol , vol.21 , pp. 5050-5062
    • Takano, A.1    Usui, I.2    Haruta, T.3    Kawahara, J.4    Uno, T.5
  • 232
    • 34047095297 scopus 로고    scopus 로고
    • The two TORCs and Akt
    • 17419990 1:CAS:528:DC%2BD2sXksVOhs7c%3D 10.1016/j.devcel.2007.03.020
    • Bhaskar PT, Hay N (2007) The two TORCs and Akt. Dev Cell 12:487-502
    • (2007) Dev Cell , vol.12 , pp. 487-502
    • Bhaskar, P.T.1    Hay, N.2
  • 233
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • 15718470 1:CAS:528:DC%2BD2MXhtlSrtbY%3D 10.1126/science.1106148
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307:1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 234
    • 61449244533 scopus 로고    scopus 로고
    • Rictor/TORC2 regulates fat metabolism, feeding, growth, and life span in Caenorhabditis elegans
    • 19240135 1:CAS:528:DC%2BD1MXivF2nt70%3D 10.1101/gad.1775409
    • Soukas AA, Kane EA, Carr CE, Melo JA, Ruvkun G (2009) Rictor/TORC2 regulates fat metabolism, feeding, growth, and life span in Caenorhabditis elegans. Genes Dev 23:496-511
    • (2009) Genes Dev , vol.23 , pp. 496-511
    • Soukas, A.A.1    Kane, E.A.2    Carr, C.E.3    Melo, J.A.4    Ruvkun, G.5
  • 235
    • 67650944993 scopus 로고    scopus 로고
    • Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
    • 19587680 1:CAS:528:DC%2BD1MXotlSgtLg%3D
    • Harrison DE, Strong R, Sharp ZD, Nelson JF, Astle CM, et al. (2009) Rapamycin fed late in life extends lifespan in genetically heterogeneous mice. Nature 460:392-395
    • (2009) Nature , vol.460 , pp. 392-395
    • Harrison, D.E.1    Strong, R.2    Sharp, Z.D.3    Nelson, J.F.4    Astle, C.M.5
  • 236
    • 70349669095 scopus 로고    scopus 로고
    • Ribosomal protein S6 kinase 1 signaling regulates mammalian life span
    • 19797661 1:CAS:528:DC%2BD1MXhtF2hs7nJ 10.1126/science.1177221
    • Selman C, Tullet JM, Wieser D, Irvine E, Lingard SJ, et al. (2009) Ribosomal protein S6 kinase 1 signaling regulates mammalian life span. Science 326:140-144
    • (2009) Science , vol.326 , pp. 140-144
    • Selman, C.1    Tullet, J.M.2    Wieser, D.3    Irvine, E.4    Lingard, S.J.5
  • 237
    • 36248931517 scopus 로고    scopus 로고
    • Nonimmunosuppressive effects of mammalian target of rapamycin inhibitors
    • 10.1016/j.trre.2007.09.003
    • Cruzado JM (2008) Nonimmunosuppressive effects of mammalian target of rapamycin inhibitors. Transplant Rev (Orlando) 22:73-81
    • (2008) Transplant Rev (Orlando) , vol.22 , pp. 73-81
    • Cruzado, J.M.1
  • 238
    • 0036691215 scopus 로고    scopus 로고
    • Effects of sirolimus on plasma lipids, lipoprotein levels, and fatty acid metabolism in renal transplant patients
    • 12177161 1:CAS:528:DC%2BD38XntFWkt7w%3D
    • Morrisett JD, Abdel-Fattah G, Hoogeveen R, Mitchell E, Ballantyne CM, et al. (2002) Effects of sirolimus on plasma lipids, lipoprotein levels, and fatty acid metabolism in renal transplant patients. J Lipid Res 43:1170-1180
    • (2002) J Lipid Res , vol.43 , pp. 1170-1180
    • Morrisett, J.D.1    Abdel-Fattah, G.2    Hoogeveen, R.3    Mitchell, E.4    Ballantyne, C.M.5
  • 239
    • 77954251401 scopus 로고    scopus 로고
    • Attenuated mTOR signaling and enhanced autophagy in adipocytes from obese patients with type 2 diabetes
    • 20386866 10.2119/molmed.2010.00023 1:CAS:528:DC%2BC3cXpsFejtbg%3D
    • Ost A, Svensson K, Ruishalme I, Brannmark C, Franck N, et al. (2010) Attenuated mTOR signaling and enhanced autophagy in adipocytes from obese patients with type 2 diabetes. Mol Med 16:235-246
    • (2010) Mol Med , vol.16 , pp. 235-246
    • Ost, A.1    Svensson, K.2    Ruishalme, I.3    Brannmark, C.4    Franck, N.5
  • 240
    • 84858753111 scopus 로고    scopus 로고
    • MTOR inhibition with rapamycin causes impaired insulin signalling and glucose uptake in human subcutaneous and omental adipocytes
    • 22333157 1:CAS:528:DC%2BC38XjtFSgtr4%3D 10.1016/j.mce.2012.01.024
    • Pereira MJ, Palming J, Rizell M, Aureliano M, Carvalho E, et al. (2012) mTOR inhibition with rapamycin causes impaired insulin signalling and glucose uptake in human subcutaneous and omental adipocytes. Mol Cell Endocrinol 355:96-105
    • (2012) Mol Cell Endocrinol , vol.355 , pp. 96-105
    • Pereira, M.J.1    Palming, J.2    Rizell, M.3    Aureliano, M.4    Carvalho, E.5
  • 241
    • 77953218866 scopus 로고    scopus 로고
    • Chronic rapamycin treatment causes glucose intolerance and hyperlipidemia by upregulating hepatic gluconeogenesis and impairing lipid deposition in adipose tissue
    • 20299475 1:CAS:528:DC%2BC3cXotFGktbo%3D 10.2337/db09-1324
    • Houde VP, Brule S, Festuccia WT, Blanchard PG, Bellmann K, et al. (2010) Chronic rapamycin treatment causes glucose intolerance and hyperlipidemia by upregulating hepatic gluconeogenesis and impairing lipid deposition in adipose tissue. Diabetes 59:1338-1348
    • (2010) Diabetes , vol.59 , pp. 1338-1348
    • Houde, V.P.1    Brule, S.2    Festuccia, W.T.3    Blanchard, P.G.4    Bellmann, K.5
  • 242
    • 8444224619 scopus 로고    scopus 로고
    • Balancing Akt with S6 K: Implications for both metabolic diseases and tumorigenesis
    • 15533996 1:CAS:528:DC%2BD2cXpvVCgu7k%3D 10.1083/jcb.200408161
    • Manning BD (2004) Balancing Akt with S6 K: implications for both metabolic diseases and tumorigenesis. J Cell Biol 167:399-403
    • (2004) J Cell Biol , vol.167 , pp. 399-403
    • Manning, B.D.1
  • 243
    • 33645795212 scopus 로고    scopus 로고
    • Proteomic analysis reveals novel molecules involved in insulin signaling pathway
    • 16602692 1:CAS:528:DC%2BD28Xhs1Whsb0%3D 10.1021/pr050391m
    • Wang Y, Li R, Du D, Zhang C, Yuan H, et al. (2006) Proteomic analysis reveals novel molecules involved in insulin signaling pathway. J Proteome Res 5:846-855
    • (2006) J Proteome Res , vol.5 , pp. 846-855
    • Wang, Y.1    Li, R.2    Du, D.3    Zhang, C.4    Yuan, H.5
  • 244
    • 71749092573 scopus 로고    scopus 로고
    • Genotype-phenotype correlation in inherited severe insulin resistance
    • 12023989 1:CAS:528:DC%2BD38XksFWmsLY%3D 10.1093/hmg/11.12.1465
    • Longo N, Wang Y, Smith SA, Langley SD, DiMeglio LA, et al. (2002) Genotype-phenotype correlation in inherited severe insulin resistance. Hum Mol Genet 11:1465-1475
    • (2002) Hum Mol Genet , vol.11 , pp. 1465-1475
    • Longo, N.1    Wang, Y.2    Smith, S.A.3    Langley, S.D.4    Dimeglio, L.A.5
  • 245
    • 1642464775 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of adipose tissue plasticity in muscle insulin receptor knockout mice
    • 14684612 1:CAS:528:DC%2BD2cXis1SisLk%3D 10.1210/en.2003-0882
    • Cariou B, Postic C, Boudou P, Burcelin R, Kahn CR, et al. (2004) Cellular and molecular mechanisms of adipose tissue plasticity in muscle insulin receptor knockout mice. Endocrinology 145:1926-1932
    • (2004) Endocrinology , vol.145 , pp. 1926-1932
    • Cariou, B.1    Postic, C.2    Boudou, P.3    Burcelin, R.4    Kahn, C.R.5
  • 246
    • 21144453387 scopus 로고    scopus 로고
    • Caveolin-3 knockout mice show increased adiposity and whole body insulin resistance, with ligand-induced insulin receptor instability in skeletal muscle
    • 15689413 1:CAS:528:DC%2BD2MXlsVymurc%3D 10.1152/ajpcell.00489.2004
    • Capozza F, Combs TP, Cohen AW, Cho YR, Park SY, et al. (2005) Caveolin-3 knockout mice show increased adiposity and whole body insulin resistance, with ligand-induced insulin receptor instability in skeletal muscle. Am J Physiol Cell Physiol 288:C1317-C1331
    • (2005) Am J Physiol Cell Physiol , vol.288
    • Capozza, F.1    Combs, T.P.2    Cohen, A.W.3    Cho, Y.R.4    Park, S.Y.5
  • 247
    • 10744221581 scopus 로고    scopus 로고
    • Increased insulin sensitivity and hypoinsulinemia in APS knockout mice
    • 14578283 1:CAS:528:DC%2BD3sXovVagtrk%3D 10.2337/diabetes.52.11.2657
    • Minami A, Iseki M, Kishi K, Wang M, Ogura M, et al. (2003) Increased insulin sensitivity and hypoinsulinemia in APS knockout mice. Diabetes 52:2657-2665
    • (2003) Diabetes , vol.52 , pp. 2657-2665
    • Minami, A.1    Iseki, M.2    Kishi, K.3    Wang, M.4    Ogura, M.5
  • 248
    • 0028032894 scopus 로고
    • Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1
    • 7969452 1:CAS:528:DyaK2cXmvFehu7k%3D 10.1038/372182a0
    • Tamemoto H, Kadowaki T, Tobe K, Yagi T, Sakura H, et al. (1994) Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1. Nature 372:182-186
    • (1994) Nature , vol.372 , pp. 182-186
    • Tamemoto, H.1    Kadowaki, T.2    Tobe, K.3    Yagi, T.4    Sakura, H.5
  • 249
    • 0030683614 scopus 로고    scopus 로고
    • Insulin resistance syndrome in mice deficient in insulin receptor substrate-1
    • 9329743 1:CAS:528:DyaK2sXmvFyltLw%3D 10.1111/j.1749-6632.1997.tb51823.x
    • Tamemoto H, Tobe K, Yamauchi T, Terauchi Y, Kaburagi Y, et al. (1997) Insulin resistance syndrome in mice deficient in insulin receptor substrate-1. Ann N Y Acad Sci 827:85-93
    • (1997) Ann N y Acad Sci , vol.827 , pp. 85-93
    • Tamemoto, H.1    Tobe, K.2    Yamauchi, T.3    Terauchi, Y.4    Kaburagi, Y.5
  • 250
    • 14644408047 scopus 로고    scopus 로고
    • Munc18c heterozygous knockout mice display increased susceptibility for severe glucose intolerance
    • 15734838 1:CAS:528:DC%2BD2MXitlegsr4%3D 10.2337/diabetes.54.3.638
    • Oh E, Spurlin BA, Pessin JE, Thurmond DC (2005) Munc18c heterozygous knockout mice display increased susceptibility for severe glucose intolerance. Diabetes 54:638-647
    • (2005) Diabetes , vol.54 , pp. 638-647
    • Oh, E.1    Spurlin, B.A.2    Pessin, J.E.3    Thurmond, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.