메뉴 건너뛰기




Volumn 36, Issue , 1996, Pages 615-658

Insulin signal transduction and the IRS proteins

Author keywords

cytokines; diabetes; SH2 domains; tyrosine kinases; tyrosine phosphorylation

Indexed keywords

CYTOKINE; GROWTH FACTOR; INSULIN; INSULIN RECEPTOR; PROTEIN; PROTEIN TYROSINE KINASE;

EID: 0029924856     PISSN: 00664251     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.pa.36.040196.003151     Document Type: Review
Times cited : (300)

References (234)
  • 1
    • 0000269388 scopus 로고
    • Epidemiology and genetics of diabetes mellitus
    • ed. CR Kahn, GC Weir, Philadelphia: Lea & Febiger. 13th ed.
    • Warram JH, Rich SS, Krolewski AS. 1995. Epidemiology and genetics of diabetes mellitus. In Joslin's Diabetes Mellitus, ed. CR Kahn, GC Weir, pp. 24-56. Philadelphia: Lea & Febiger. 13th ed.
    • (1995) Joslin's Diabetes Mellitus , pp. 24-56
    • Warram, J.H.1    Rich, S.S.2    Krolewski, A.S.3
  • 2
    • 0026456964 scopus 로고
    • The insulin-sensitive glucose transporter
    • Birnbaum MJ. 1993. The insulin-sensitive glucose transporter. Int. Rev. Cytol. 137:239-97
    • (1993) Int. Rev. Cytol. , vol.137 , pp. 239-297
    • Birnbaum, M.J.1
  • 8
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • 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 313:756-61
    • (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
  • 9
    • 0018757089 scopus 로고
    • Regulation of insulin receptors and insulin responsiveness in 3T3-L1 fatty fibroblasts
    • Karlsson FA, Grunfeld C, Kahn CR, Roth J. 1979. Regulation of insulin receptors and insulin responsiveness in 3T3-L1 fatty fibroblasts. Endocrinology 104:1383-92
    • (1979) Endocrinology , vol.104 , pp. 1383-1392
    • Karlsson, F.A.1    Grunfeld, C.2    Kahn, C.R.3    Roth, J.4
  • 10
    • 0024650994 scopus 로고
    • The casacde of autophosphorylation in the β-subunit of the insulin receptor
    • White MF, Kahn CR. 1989. The casacde of autophosphorylation in the β-subunit of the insulin receptor. J. Cell. Biochem. 39:429-41
    • (1989) J. Cell. Biochem. , vol.39 , pp. 429-441
    • White, M.F.1    Kahn, C.R.2
  • 11
    • 0027277107 scopus 로고
    • Insulin stimulates serine and tyrosine phosphorylation in the juxtamembrane region of the insulin receptor
    • Feener EP, Backer JM, King GL, Wilden PA, Sun XJ, et al. 1993. Insulin stimulates serine and tyrosine phosphorylation in the juxtamembrane region of the insulin receptor. J. Biol. Chem. 268: 11256-64
    • (1993) J. Biol. Chem. , vol.268 , pp. 11256-11264
    • Feener, E.P.1    Backer, J.M.2    King, G.L.3    Wilden, P.A.4    Sun, X.J.5
  • 12
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White MF, Kahn CR. 1994. The insulin signaling system. J. Biol. Chem. 269:1-5
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-5
    • White, M.F.1    Kahn, C.R.2
  • 13
    • 0023905461 scopus 로고
    • Properties of a human insulin receptor with a COOH-terminal truncation. I. Insulin binding, autophosphorylation and endocytosis
    • McClain D, Maegawa H, Levy J, Huecksteadt T, Dull TJ, et al. 1988. Properties of a human insulin receptor with a COOH-terminal truncation. I. Insulin binding, autophosphorylation and endocytosis. J. Biol. Chem. 263: 8904-12
    • (1988) J. Biol. Chem. , vol.263 , pp. 8904-8912
    • McClain, D.1    Maegawa, H.2    Levy, J.3    Huecksteadt, T.4    Dull, T.J.5
  • 14
    • 0023907193 scopus 로고
    • Properties of a human insulin receptor with a COOH-terminal trancation II. Truncated receptors have normal kinase activity but are defective in signaling metabolic effects
    • Maegawa H, McClain DA, Freidenberg G, Olefsky JM, Napier M, et al. 1988. Properties of a human insulin receptor with a COOH-terminal trancation II. Truncated receptors have normal kinase activity but are defective in signaling metabolic effects. J. Biol. Chem. 263: 8912-17
    • (1988) J. Biol. Chem. , vol.263 , pp. 8912-8917
    • Maegawa, H.1    McClain, D.A.2    Freidenberg, G.3    Olefsky, J.M.4    Napier, M.5
  • 15
    • 0023240345 scopus 로고
    • Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin
    • Chou CK, Dull TJ, Russell DS, Gherzi R, Lebwohl D, et al. 1987. Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin. J. Biol. Chem. 262: 1842-47
    • (1987) J. Biol. Chem. , vol.262 , pp. 1842-1847
    • Chou, C.K.1    Dull, T.J.2    Russell, D.S.3    Gherzi, R.4    Lebwohl, D.5
  • 16
    • 0023665224 scopus 로고
    • A mutant insulin receptor with defective tyrosine kinase displays no biological activity and does not undergo endocytosis
    • McClain DA, Maegawa H, Lee J, Dull TJ, Ullrich A, Olefsky JM. 1987. A mutant insulin receptor with defective tyrosine kinase displays no biological activity and does not undergo endocytosis. J. Biol. Chem. 262:14663-71
    • (1987) J. Biol. Chem. , vol.262 , pp. 14663-14671
    • McClain, D.A.1    Maegawa, H.2    Lee, J.3    Dull, T.J.4    Ullrich, A.5    Olefsky, J.M.6
  • 17
    • 0024323165 scopus 로고
    • Human diabetes associated with a mutation in the tyrosine kinase domain of the insulin receptor
    • Odawara M, Kadowaki T, Yamamoto R, Shibasaki Y, Tobe K, et al. 1989. Human diabetes associated with a mutation in the tyrosine kinase domain of the insulin receptor. Science 245:66-68
    • (1989) Science , vol.245 , pp. 66-68
    • Odawara, M.1    Kadowaki, T.2    Yamamoto, R.3    Shibasaki, Y.4    Tobe, K.5
  • 18
    • 0024995838 scopus 로고
    • A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance
    • Moller DE, Yokota A, White MF, Pazianos AG, Flier JS. 1990. A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance. J. Biol. Chem. 265:14979-85
    • (1990) J. Biol. Chem. , vol.265 , pp. 14979-14985
    • Moller, D.E.1    Yokota, A.2    White, M.F.3    Pazianos, A.G.4    Flier, J.S.5
  • 19
    • 0023188325 scopus 로고
    • After insulin binds
    • Rosen OM. 1987. After insulin binds. Science 237:1452-58
    • (1987) Science , vol.237 , pp. 1452-1458
    • Rosen, O.M.1
  • 20
  • 21
    • 0023875702 scopus 로고
    • Synthesis, purification and characterization of the cytoplasmic domain of the human insulin recpetor using a baculovirus expression system
    • Herrera R, Lebwohl D, Garcia de Herreros A, Kallen RG, Rosen OM. 1988. Synthesis, purification and characterization of the cytoplasmic domain of the human insulin recpetor using a baculovirus expression system. J. Biol. Chem. 263:5560-68
    • (1988) J. Biol. Chem. , vol.263 , pp. 5560-5568
    • Herrera, R.1    Lebwohl, D.2    Garcia De Herreros, A.3    Kallen, R.G.4    Rosen, O.M.5
  • 23
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-1 receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling
    • DeMeyts P. 1995. The structural basis of insulin and insulin-like growth factor-1 receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia 37:S135-48
    • (1995) Diabetologia , vol.37
    • DeMeyts, P.1
  • 24
    • 0026053772 scopus 로고
    • Transdominant inhibition of tyrosine kinase activity in mutant insulin/insulin-like growth factor I hybrid receptors
    • Treadway JL, Morrison BD, Soos MA, Siddle K, Olefsky J, et al. 1991. Transdominant inhibition of tyrosine kinase activity in mutant insulin/insulin-like growth factor I hybrid receptors. Proc. Natl. Acad. Sci. USA 88:214-18
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 214-218
    • Treadway, J.L.1    Morrison, B.D.2    Soos, M.A.3    Siddle, K.4    Olefsky, J.5
  • 25
    • 0027415084 scopus 로고
    • Insulin receptor autophosphorylation occurs asymmetrically
    • Lee J, O'Hare T, Pilch PF, Shoelson SE. 1993 Insulin receptor autophosphorylation occurs asymmetrically. J. Biol. Chem. 268:4092-98
    • (1993) J. Biol. Chem. , vol.268 , pp. 4092-4098
    • Lee, J.1    O'Hare, T.2    Pilch, P.F.3    Shoelson, S.E.4
  • 26
    • 0026649556 scopus 로고
    • Transmembrane signaling by the human insulin receptor kinase. Relationship between intramolecular β subunit trans- and cis-autophosphorylation and substrate kinase activation
    • Fratalli AL, Treadway JL,. Pessin JE. 1992. Transmembrane signaling by the human insulin receptor kinase. Relationship between intramolecular β subunit trans- and cis-autophosphorylation and substrate kinase activation. J. Biol. Chem. 267:19521-28
    • (1992) J. Biol. Chem. , vol.267 , pp. 19521-19528
    • Fratalli, A.L.1    Treadway, J.L.2    Pessin, J.E.3
  • 27
    • 0027339764 scopus 로고
    • BpaB25 insulins. Photoactivatable analogues that quantitatively cross-link, radiolabel, and activate the insulin receptor
    • Shoelson SE, Lee J, Lynch CS, Backer JM, Pilch PF. 1993. BpaB25 insulins. Photoactivatable analogues that quantitatively cross-link, radiolabel, and activate the insulin receptor. J. Biol. Chem. 268:4085-91
    • (1993) J. Biol. Chem. , vol.268 , pp. 4085-4091
    • Shoelson, S.E.1    Lee, J.2    Lynch, C.S.3    Backer, J.M.4    Pilch, P.F.5
  • 28
    • 0027186439 scopus 로고
    • Substitution of the erB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1
    • Cheatham B, Shoelson SE, Yamada K, Goncalves E, Kahn CR. 1993. Substitution of the erB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1. Proc. Natl. Acad. Sci. USA 90:7336-40
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7336-7340
    • Cheatham, B.1    Shoelson, S.E.2    Yamada, K.3    Goncalves, E.4    Kahn, C.R.5
  • 29
    • 0023686033 scopus 로고
    • Signal transduction by allosteric receptor oligomerization
    • Schlessinger J. 1988. Signal transduction by allosteric receptor oligomerization. Trends Biochem. Sci. 13:443-47
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 443-447
    • Schlessinger, J.1
  • 30
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the β-subunit activates the insulin receptor
    • White MF, Shoelson SE, Keutmann H, Kahn CR. 1988. A cascade of tyrosine autophosphorylation in the β-subunit activates the insulin receptor. J. Biol. Chem. 263:2969-80
    • (1988) J. Biol. Chem. , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4
  • 31
    • 0025372470 scopus 로고
    • Characterization of the insulin receptor with an in vitro mutation at tyrosine 1146: Evidence for separate insulin receptor signals regulating cellular metabolism and growth
    • Wilden PA, Backer JM, Kahn CR, Cahill DA, Schroeder GJ, White MF. 1990. Characterization of the insulin receptor with an in vitro mutation at tyrosine 1146: evidence for separate insulin receptor signals regulating cellular metabolism and growth. Proc. Natl. Acad. Sci. USA 87:3358-62
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3358-3362
    • Wilden, P.A.1    Backer, J.M.2    Kahn, C.R.3    Cahill, D.A.4    Schroeder, G.J.5    White, M.F.6
  • 32
    • 0026748806 scopus 로고
    • The role of insulin receptor kinase domain autophosphorylation in receptor-mediated activities
    • Wilden PA, Siddle K, Haring E, Backer JM, White MF, Kahn CR. 1992. The role of insulin receptor kinase domain autophosphorylation in receptor-mediated activities. J. Biol. Chem. 267: 13719-27
    • (1992) J. Biol. Chem. , vol.267 , pp. 13719-13727
    • Wilden, P.A.1    Siddle, K.2    Haring, E.3    Backer, J.M.4    White, M.F.5    Kahn, C.R.6
  • 33
    • 0023022750 scopus 로고
    • Autophosphorylation of the insulin receptor in vitro. Designation of phosphorylation sites and correlation with receptor kinase activation
    • 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: 11980-85
    • (1986) J. Biol. Chem. , vol.261 , pp. 11980-11985
    • Herrera, R.1    Rosen, O.M.2
  • 35
    • 0024409786 scopus 로고
    • Nonphpsphorylatable substrate analogs selectively block autophosphorylation and activation of the insulin receptor, epidermal growth factor receptor and pp60v-src kinases
    • Shoelson SE, White MF, Kahn CR. 1989. Nonphpsphorylatable substrate analogs selectively block autophosphorylation and activation of the insulin receptor, epidermal growth factor receptor and pp60v-src kinases. J. Biol. Chem. 264:7831-36
    • (1989) J. Biol. Chem. , vol.264 , pp. 7831-7836
    • Shoelson, S.E.1    White, M.F.2    Kahn, C.R.3
  • 36
    • 0025951971 scopus 로고
    • Transmembrane signalling by insulin via an insulin receptor mutated at tyrosines 1158, 1162, and 1163
    • Rafaeloff R, Maddux BA, Brunetti A, Sbraccia P, Sung CK, et al. 1991. Transmembrane signalling by insulin via an insulin receptor mutated at tyrosines 1158, 1162, and 1163. Biochem. Biophys. Res. Commun. 179:912-18
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 912-918
    • Rafaeloff, R.1    Maddux, B.A.2    Brunetti, A.3    Sbraccia, P.4    Sung, C.K.5
  • 37
    • 0026742983 scopus 로고
    • Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function
    • Wilden PA, Kahn CR, Siddle K, White MF. 1992. Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function. J. Biol. Chem. 267:16660-68
    • (1992) J. Biol. Chem. , vol.267 , pp. 16660-16668
    • Wilden, P.A.1    Kahn, C.R.2    Siddle, K.3    White, M.F.4
  • 38
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard SR, Wei L, Ellis L, Hendrickson WA. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372:746-54
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 40
    • 0028938721 scopus 로고
    • Catalytic specificity of protein-tyrosine kinases is critical for selective signalling
    • Songyang Z, Carraway KL III, Eck MJ, Harrison SC, Feldman RA, et al. 1995. Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature 373:536-39
    • (1995) Nature , vol.373 , pp. 536-539
    • Songyang, Z.1    Carraway III, K.L.2    Eck, M.J.3    Harrison, S.C.4    Feldman, R.A.5
  • 41
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch CA, Anderson DJ, Moran MF, Ellis C, Pawson T. 1991. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252:668-74
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.J.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 42
    • 0027516706 scopus 로고
    • IRS-1 is a common element in insulin and insulin-like growth factor-1 signaling to the phosphatidylinositol 3′-kinase
    • Myers MG Jr, Sun XJ, Cheatham B, Jachna BR, Glasheen EM, et al. 1993. IRS-1 is a common element in insulin and insulin-like growth factor-1 signaling to the phosphatidylinositol 3′-kinase. Endocrinology 132:1421-30
    • (1993) Endocrinology , vol.132 , pp. 1421-1430
    • Myers Jr., M.G.1    Sun, X.J.2    Cheatham, B.3    Jachna, B.R.4    Glasheen, E.M.5
  • 43
    • 0022347547 scopus 로고
    • Insulin rapidly stimulates tyrosine phosphorylation of a Mr 185,000 protein in intact cells
    • White MF, Maron R, Kahn CR. 1985. Insulin rapidly stimulates tyrosine phosphorylation of a Mr 185,000 protein in intact cells. Nature 318:183-86
    • (1985) Nature , vol.318 , pp. 183-186
    • White, M.F.1    Maron, R.2    Kahn, C.R.3
  • 44
    • 0023655603 scopus 로고
    • Characterization of an endogenous substrate of the insulin receptor in cultured cells
    • White MF, Stegmann EW, Dull TJ, Ullrich A, Kahn CR. 1987. Characterization of an endogenous substrate of the insulin receptor in cultured cells. J. Biol. Chem. 262:9769-77
    • (1987) J. Biol. Chem. , vol.262 , pp. 9769-9777
    • White, M.F.1    Stegmann, E.W.2    Dull, T.J.3    Ullrich, A.4    Kahn, C.R.5
  • 45
    • 0023227345 scopus 로고
    • Insulin stimulates phosphorylation of a 120-kDa glycoprotein substrate (pp120) for the receptor-associated protein kinase in intact H-35 hepatoma cells
    • Perrotti N, Accili D, Marcus Samuels B, Rees Jones RW, Taylor SI. 1987. Insulin stimulates phosphorylation of a 120-kDa glycoprotein substrate (pp120) for the receptor-associated protein kinase in intact H-35 hepatoma cells. Proc. Natl. Acad. Sci. USA 84:3137-40
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3137-3140
    • Perrotti, N.1    Accili, D.2    Marcus Samuels, B.3    Rees Jones, R.W.4    Taylor, S.I.5
  • 46
    • 0025138734 scopus 로고
    • Hepatocyte plasma membrane ecto-ATPase (pp120/HA4) is a substrate for tyrosine kinase activity of the insulin receptor
    • Margolis RN, Schell MJ, Taylor SI, Hubbard AL. 1990. Hepatocyte plasma membrane ecto-ATPase (pp120/HA4) is a substrate for tyrosine kinase activity of the insulin receptor. Biochem. Biophys. Res. Commun. 166:562-66
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 562-566
    • Margolis, R.N.1    Schell, M.J.2    Taylor, S.I.3    Hubbard, A.L.4
  • 47
    • 0027458375 scopus 로고
    • pp120/ecto-ATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isoforms
    • Najjar SM, Accili D, Philippe N, Jernberg J, Margolis R, Taylor SI. 1993. pp120/ecto-ATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isoforms. J. Biol. Chem. 268: 1201-6
    • (1993) J. Biol. Chem. , vol.268 , pp. 1201-1206
    • Najjar, S.M.1    Accili, D.2    Philippe, N.3    Jernberg, J.4    Margolis, R.5    Taylor, S.I.6
  • 48
    • 0027417484 scopus 로고
    • The insulin-elicited 60-kDa phosphotyrosine protein in rat adipocytes is associated with phosphatidylinositol 3-kinase
    • Lavan BE, Lienhard GE. 1993. The insulin-elicited 60-kDa phosphotyrosine protein in rat adipocytes is associated with phosphatidylinositol 3-kinase. J. Biol. Chem. 268:5921-28
    • (1993) J. Biol. Chem. , vol.268 , pp. 5921-5928
    • Lavan, B.E.1    Lienhard, G.E.2
  • 49
    • 0028232158 scopus 로고
    • Role of p85 subunit of phosphatidylinositol-3-kinase as an adaptor molecule linking the insulin receptor, p62, and GTPase-activating protein
    • Sung CK, Sanchez-Margalet V, Goldfine ID. 1994. Role of p85 subunit of phosphatidylinositol-3-kinase as an adaptor molecule linking the insulin receptor, p62, and GTPase-activating protein. J. Biol. Chem. 269:12503-7
    • (1994) J. Biol. Chem. , vol.269 , pp. 12503-12507
    • Sung, C.K.1    Sanchez-Margalet, V.2    Goldfine, I.D.3
  • 50
    • 0023731888 scopus 로고
    • Effect of vanadate on the cellular accumulation of pp15, an apparent product of insulin receptor tyrosine kinase action
    • Bernier M, Laird DM, Lane MD. 1988. Effect of vanadate on the cellular accumulation of pp15, an apparent product of insulin receptor tyrosine kinase action. J. Biol. Chem. 263:13626-34
    • (1988) J. Biol. Chem. , vol.263 , pp. 13626-13634
    • Bernier, M.1    Laird, D.M.2    Lane, M.D.3
  • 51
    • 0024269622 scopus 로고
    • Identification of phosphorylated 422(aP2) protein as pp15, the 15-kilodalton target of the insulin receptor tyrosine kinase in 3T3-L1 adipocytes
    • Hresko RC, Bernier M, Hoffman RD, Flores Riveros JR, Liao K, et al. 1988. Identification of phosphorylated 422(aP2) protein as pp15, the 15-kilodalton target of the insulin receptor tyrosine kinase in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. USA 85:8835-39
    • (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
  • 52
    • 0028928447 scopus 로고
    • Insulin-dependent tyrosine phosphorylation of the vav proto-oncogene product in cells of hematopoietic origin
    • Uddin S, Katzav S, White MF, Platanias LC. 1995. Insulin-dependent tyrosine phosphorylation of the vav proto-oncogene product in cells of hematopoietic origin. J. Biol. Chem. 270:7712-16
    • (1995) J. Biol. Chem. , vol.270 , pp. 7712-7716
    • Uddin, S.1    Katzav, S.2    White, M.F.3    Platanias, L.C.4
  • 53
    • 0027207287 scopus 로고
    • Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation
    • Gulbins E, Coggeshall KM, Baier G, Katzav S, Burn P, Altman A. 1993. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation [see comments]. Science 260:822-25
    • (1993) Science , vol.260 , pp. 822-825
    • Gulbins, E.1    Coggeshall, K.M.2    Baier, G.3    Katzav, S.4    Burn, P.5    Altman, A.6
  • 54
    • 0027570504 scopus 로고
    • Vav: A potential link between tyrosine kinases and ras-like GTPases in hematopoietic cell signaling
    • Hu P, Margolis B, Schlessinger J. 1993. Vav: a potential link between tyrosine kinases and ras-like GTPases in hematopoietic cell signaling. BioEssays 15: 179-83
    • (1993) BioEssays , vol.15 , pp. 179-183
    • Hu, P.1    Margolis, B.2    Schlessinger, J.3
  • 55
    • 0026777369 scopus 로고
    • A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
    • Pellici G, Lanfrancone L, Grignani F, McGlade J, Cavallo F, et al. 1992. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70:93-104
    • (1992) Cell , vol.70 , pp. 93-104
    • Pellici, G.1    Lanfrancone, L.2    Grignani, F.3    McGlade, J.4    Cavallo, F.5
  • 56
    • 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
    • Skolnik EY, Lee CH, Batzer A, Vicentini LM, 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. 12:1929-36
    • (1993) EMBO J. , vol.12 , pp. 1929-1936
    • Skolnik, E.Y.1    Lee, C.H.2    Batzer, A.3    Vicentini, L.M.4    Zhou, M.5
  • 58
    • 0025837881 scopus 로고
    • Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase
    • Rothenberg PL, Lane WS, Karasik A, Backer J, White M, Kahn CR. 1991. Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase. J. Biol. Chem. 266:8302-11
    • (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    Kahn, C.R.6
  • 59
    • 0025813375 scopus 로고
    • The structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
    • Sun XJ, Rothenberg P, Kahn CR. Backer JM, Araki E, et al. 1991. The 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
  • 61
    • 0026605216 scopus 로고
    • Cloning and increased expression of an insulin receptor substrate-1-like gene in human hepatocellular carcinoma
    • Nishiyama M, Wands JR. 1992. Cloning and increased expression of an insulin receptor substrate-1-like gene in human hepatocellular carcinoma. Biochem. Biophys. Res. Commun. 183:280-85
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 280-285
    • Nishiyama, M.1    Wands, J.R.2
  • 62
    • 0025879715 scopus 로고
    • Isolation and characterization of the 160,000-Dalton phosphotyrosyl protein, a putative participant in insulin signaling
    • Keller SR, Kitagawa K, Aebersold RH, Lienhard GE, Garner CW. 1991. Isolation and characterization of the 160,000-Dalton phosphotyrosyl protein, a putative participant in insulin signaling. J. Biol. Chem. 266:12817-20
    • (1991) J. Biol. Chem. , vol.266 , pp. 12817-12820
    • Keller, S.R.1    Kitagawa, K.2    Aebersold, R.H.3    Lienhard, G.E.4    Garner, C.W.5
  • 63
    • 0027512629 scopus 로고
    • The insulin-elicited 160 kDa phosphotyrosine protein in mouse adipocytes is an insulin receptor substrate 1: Identification by cloning
    • Keller SR, Aebersold RH, Garner CW, Lienhard GE. 1993. The insulin-elicited 160 kDa phosphotyrosine protein in mouse adipocytes is an insulin receptor substrate 1: identification by cloning. Biochim. Biophys. Acta 1172:323-26
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 323-326
    • Keller, S.R.1    Aebersold, R.H.2    Garner, C.W.3    Lienhard, G.E.4
  • 64
    • 0029067502 scopus 로고
    • Molecular cloning of an amphibian IRS-1-like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation
    • Liu XJ, Sorisky A, Zhu L, Pawson A. 1995. Molecular cloning of an amphibian IRS-1-like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation. Mol. Cell. Biol. 15:3563-70
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3563-3570
    • Liu, X.J.1    Sorisky, A.2    Zhu, L.3    Pawson, A.4
  • 65
    • 0026655777 scopus 로고
    • Insulin stimulates tyrosine phosphorylation of multiple high molecular weight substrates in FAO hepatoma cells
    • Miralpeix M, Sun XJ, Backer JM, Myers MG Jr, Araki E, White MF. 1992. Insulin stimulates tyrosine phosphorylation of multiple high molecular weight substrates in FAO hepatoma cells. Biochemistry 31:9031-39
    • (1992) Biochemistry , vol.31 , pp. 9031-9039
    • Miralpeix, M.1    Sun, X.J.2    Backer, J.M.3    Myers Jr., M.G.4    Araki, E.5    White, M.F.6
  • 67
    • 0027262352 scopus 로고
    • Common elements in IL4 and insulin signaling pathways in factor dependent hematopoietic cells
    • Wang LM, Keegan AD, Li WQ, Lienhard GE, Pacini S, et al. 1993. Common elements in IL4 and insulin signaling pathways in factor dependent hematopoietic cells. Proc. Natl. Acad. Sci. USA 90:4032-36
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4032-4036
    • Wang, L.M.1    Keegan, A.D.2    Li, W.Q.3    Lienhard, G.E.4    Pacini, S.5
  • 69
  • 70
    • 0028237039 scopus 로고
    • A biochemical function for ras - At last
    • Hall A. 1994. A biochemical function for ras - at last. Science 264:1413-14
    • (1994) Science , vol.264 , pp. 1413-1414
    • Hall, A.1
  • 71
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of Shc and IRS-1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain
    • Gustafson TA, He W, Craparo A, Schaub CD, O'Neill TJ. 1995. Phosphotyrosine-dependent interaction of Shc and IRS-1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15:2500-8
    • (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
  • 72
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh WM, Williams LT. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266:1862-65
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 73
    • 0029640799 scopus 로고
    • A phosphotyrosine interaction domain
    • Bork P, Margolis B. 1995. A phosphotyrosine interaction domain. Cell 80: 693-94
    • (1995) Cell , vol.80 , pp. 693-694
    • Bork, P.1    Margolis, B.2
  • 74
    • 0029040133 scopus 로고
    • The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor
    • Batzer AG, Blaikie P, Nelson K, Schlessinger J, Margolis B. 1995. The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor. Mol. Cell. Biol. 15:4403-9
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4403-4409
    • Batzer, A.G.1    Blaikie, P.2    Nelson, K.3    Schlessinger, J.4    Margolis, B.5
  • 75
    • 0028888604 scopus 로고
    • The PTB domain: A new protein module implicated in signal transduction
    • van der Geer P, Pawson T. 1995. The PTB domain: a new protein module implicated in signal transduction. Trends Biochem. Sci. 20:277-80
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 277-280
    • Van Der Geer, P.1    Pawson, T.2
  • 76
    • 0028219966 scopus 로고
    • An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth
    • Keegan AD, Nelms K, White M, Wang LM, Pierce JH, Paul WE. 1994. An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth. Cell 76:811-20
    • (1994) Cell , vol.76 , pp. 811-820
    • Keegan, A.D.1    Nelms, K.2    White, M.3    Wang, L.M.4    Pierce, J.H.5    Paul, W.E.6
  • 79
    • 0028282967 scopus 로고
    • Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1
    • Sugimoto S, Wandless TJ, Shoelson SE, Neel BG, Walsh CT. 1994. Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1. J. Biol. Chem. 269:13614-22
    • (1994) J. Biol. Chem. , vol.269 , pp. 13614-13622
    • Sugimoto, S.1    Wandless, T.J.2    Shoelson, S.E.3    Neel, B.G.4    Walsh, C.T.5
  • 80
    • 0028854920 scopus 로고
    • Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains
    • Pluskey S, Wandless TJ, Walsh CT, Shoelson SE. 1995. Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains. J. Biol. Chem 270:2897-900
    • (1995) J. Biol. Chem , vol.270 , pp. 2897-2900
    • Pluskey, S.1    Wandless, T.J.2    Walsh, C.T.3    Shoelson, S.E.4
  • 81
    • 0027421453 scopus 로고
    • The insulin receptor substrate (IRS-1) is a PEST protein that is susceptible to calpain degradation in vitro
    • Smith LK, Bradshaw M, Croall DE, Garner CW. 1993. The insulin receptor substrate (IRS-1) is a PEST protein that is susceptible to calpain degradation in vitro. Biochem. Biophys. Res. Commun. 196:767-72
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 767-772
    • Smith, L.K.1    Bradshaw, M.2    Croall, D.E.3    Garner, C.W.4
  • 84
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domain
    • Hanks SK, Quinn AM, Hunter T. 1990. The protein kinase family: conserved features and deduced phylogeny of the catalytic domain. Science 241:42-52
    • (1990) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 86
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D. 1995. Modular binding domains in signal transduction proteins. Cell 80:237-48
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 87
    • 0027940655 scopus 로고
    • SH2 and SH3 domains as molecular adhesives: The interactions of Crk and Abl
    • Feller SM, Ren R. Hanafusa H, Baltimore D. 1994. SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl. Trends Biochem. Sci. 19:453-58
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 453-458
    • Feller, S.M.1    Ren, R.2    Hanafusa, H.3    Baltimore, D.4
  • 88
    • 0028980989 scopus 로고
    • Growth hormone, interferon-gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1
    • Argetsinger LS, Hsu GW, Myers MG Jr, Billestrup N, White MF, Carter-Su C. 1995. Growth hormone, interferon-gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1. J. Biol. Chem. 270:14685-92
    • (1995) J. Biol. Chem. , vol.270 , pp. 14685-14692
    • Argetsinger, L.S.1    Hsu, G.W.2    Myers Jr., M.G.3    Billestrup, N.4    White, M.F.5    Carter-Su, C.6
  • 89
    • 0027942503 scopus 로고
    • Growth hormone stimulates tyrosine phosphorylation of insulin receptor substrate-1
    • Souza SC, Frick GP, Yip R, Lobo RB, Tai L-R, Goodman HM. 1994. Growth hormone stimulates tyrosine phosphorylation of insulin receptor substrate-1. J. Biol. Chem. 269:30085-88
    • (1994) J. Biol. Chem. , vol.269 , pp. 30085-30088
    • Souza, S.C.1    Frick, G.P.2    Yip, R.3    Lobo, R.B.4    Tai, L.-R.5    Goodman, H.M.6
  • 90
    • 0028910216 scopus 로고
    • Growth hormone stimulates the tyrosine phosphorylation of the insulin receptor substrate-1 and its association with phosphatidylinositol 3-kinase in primary adipocytes
    • Ridderstale M, Degerman E, Tornqvist H. 1995. Growth hormone stimulates the tyrosine phosphorylation of the insulin receptor substrate-1 and its association with phosphatidylinositol 3-kinase in primary adipocytes. J. Biol. Chem. 27&3471-74
    • (1995) J. Biol. Chem. , vol.27 , pp. 3471-3474
    • Ridderstale, M.1    Degerman, E.2    Tornqvist, H.3
  • 91
    • 0028982917 scopus 로고
    • Interferon-alpha engages IRS-signaling proteins to regulate the phosphatidylinositol 3-kinase
    • Uddin S, Yenush LP, Sun XJ, Sweet ME, White MF, Platanias LC. 1995. Interferon-alpha engages IRS-signaling proteins to regulate the phosphatidylinositol 3-kinase. J. Biol. Chem. 270: 15938-41
    • (1995) J. Biol. Chem. , vol.270 , pp. 15938-15941
    • Uddin, S.1    Yenush, L.P.2    Sun, X.J.3    Sweet, M.E.4    White, M.F.5    Platanias, L.C.6
  • 92
    • 0023814924 scopus 로고
    • Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission bul does not affect its tyrosine kinase activity
    • White MF, Livingston JN, Backer JM, Lauris V, Dull TJ, et al. 1988. Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission bul does not affect its tyrosine kinase activity. Cell 54:641-49
    • (1988) Cell , vol.54 , pp. 641-649
    • White, M.F.1    Livingston, J.N.2    Backer, J.M.3    Lauris, V.4    Dull, T.J.5
  • 93
    • 0024997853 scopus 로고
    • Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor α-subuint
    • Backer JM, Kahn CR, Cahill DA, Ullrich A, White MF. 1990. Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor α-subuint. J. Biol. Chem. 265: 16450-54
    • (1990) J. Biol. Chem. , vol.265 , pp. 16450-16454
    • Backer, J.M.1    Kahn, C.R.2    Cahill, D.A.3    Ullrich, A.4    White, M.F.5
  • 94
    • 0025819773 scopus 로고
    • The cytoplasmic juxtamembrane region of the insulin receptor: A critical role in ATP binding, endogenous substrate phosphorylauon, and insulin-stimulated bioeffects in CHO cells
    • Backer JM, Schroeder GG, Cahill DA, Ullrich A, Siddle K, White MF. 1991. The cytoplasmic juxtamembrane region of the insulin receptor: a critical role in ATP binding, endogenous substrate phosphorylauon, and insulin-stimulated bioeffects in CHO cells. Biochemistry 300:6366-72
    • (1991) Biochemistry , vol.300 , pp. 6366-6372
    • Backer, J.M.1    Schroeder, G.G.2    Cahill, D.A.3    Ullrich, A.4    Siddle, K.5    White, M.F.6
  • 95
    • 0027969225 scopus 로고
    • Characterization of an interaction between insulin receptor substrate-1 and the insulin receptor by using the two-hybrid system
    • O'Neill TJ, Craparo A, Gustafson TA. 1994. Characterization of an interaction between insulin receptor substrate-1 and the insulin receptor by using the two-hybrid system. Mol. Cell. Biol. 14:6433-42
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6433-6442
    • O'Neill, T.J.1    Craparo, A.2    Gustafson, T.A.3
  • 96
    • 0029074148 scopus 로고
    • Non-SH2 domains within the insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor 1 receptor
    • Craparo A, O'Neill TJ, Gustafson TA. 1995. Non-SH2 domains within the insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor 1 receptor. J. Biol. Chem. 270:15639-43
    • (1995) J. Biol. Chem. , vol.270 , pp. 15639-15643
    • Craparo, A.1    O'Neill, T.J.2    Gustafson, T.A.3
  • 98
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh WM, Turck CW, Williams LT. 1995. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268:1177-79
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 99
    • 0027456952 scopus 로고
    • Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells
    • Roth D, Morgan A, Burgoyne RJD. 1993. Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. FEBS Lett. 320:207-10
    • (1993) FEBS Lett. , vol.320 , pp. 207-210
    • Roth, D.1    Morgan, A.2    Burgoyne, R.J.D.3
  • 100
    • 0028568639 scopus 로고
    • A region in she distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
    • Blaikie P, Immanuel D, Wu J, Li N, Yajnik V, Margolis B. 1994. A region in she distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269: 32031-34
    • (1994) J. Biol. Chem. , vol.269 , pp. 32031-32034
    • Blaikie, P.1    Immanuel, D.2    Wu, J.3    Li, N.4    Yajnik, V.5    Margolis, B.6
  • 101
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
    • Ferguson KM, Lemmon MA, Schless-inger J, Sigler PB. 1994. Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell 79:199-2 09
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schless-inger, J.3    Sigler, P.B.4
  • 103
    • 0027305921 scopus 로고
    • Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice
    • Rawlings DJ, Saffran DC, Tsukada S, et al. 1993. Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice. Science 261:358-61
    • (1993) Science , vol.261 , pp. 358-361
    • Rawlings, D.J.1    Saffran, D.C.2    Tsukada, S.3
  • 104
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol 4,5-bisphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. 1994. Pleckstrin homology domains bind to phosphatidylinositol 4,5-bisphosphate. Nature 371:168-70
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 105
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane assocaition and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G-beta/gamma sub units and lipid
    • Pitcher JA, Touhara K, Payne ES, Lefkowitz RJ. 1995. Pleckstrin homology domain-mediated membrane assocaition and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G-beta/gamma sub units and lipid. J. Biol. Chem. 270: 11707-10
    • (1995) J. Biol. Chem. , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 106
    • 0028800798 scopus 로고
    • Dynamics of signaling during insulin-stimulated endocytosis of its receptor in adipocytes
    • Kublaoui B, Lee J, Pilch PF. 1995. Dynamics of signaling during insulin-stimulated endocytosis of its receptor in adipocytes. J. Biol. Chem. 270:59-65
    • (1995) J. Biol. Chem. , vol.270 , pp. 59-65
    • Kublaoui, B.1    Lee, J.2    Pilch, P.F.3
  • 108
    • 0028270938 scopus 로고
    • Inhibition of G protein-coupled receptor signaling by expression of cytoplasmic domains of the receptor
    • Hawes BE, Luttrell LM, Exum ST, Lefkowitz RJ. 1994. Inhibition of G protein-coupled receptor signaling by expression of cytoplasmic domains of the receptor. J. Biol. Chem. 269:15776-85
    • (1994) J. Biol. Chem. , vol.269 , pp. 15776-15785
    • Hawes, B.E.1    Luttrell, L.M.2    Exum, S.T.3    Lefkowitz, R.J.4
  • 110
    • 0028987271 scopus 로고
    • G-beta-gamma interactions with PH domains and Ras-MAPK signaling pathways
    • Inglese J, Koch WJ, Touhara K, Lefkowitz RJ. 1995. G-beta-gamma interactions with PH domains and Ras-MAPK signaling pathways. Trends Biochem. Sci. 20:151-56
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 151-156
    • Inglese, J.1    Koch, W.J.2    Touhara, K.3    Lefkowitz, R.J.4
  • 111
    • 0026698924 scopus 로고
    • Crystal structrue of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    • Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, et al. 1992. Crystal structrue of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358:646-53
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1    Kominos, D.2    Robertson, S.C.3    Pant, N.4    Baltimore, D.5
  • 112
    • 0026665009 scopus 로고
    • Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3 OH-kinase
    • Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, et al. 1992. Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3 OH-kinase. Nature 358:684-87
    • (1992) Nature , vol.358 , pp. 684-687
    • Booker, G.W.1    Breeze, A.L.2    Downing, A.K.3    Panayotou, G.4    Gout, I.5
  • 113
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures, of the complexed and peptide-free forms
    • Waksman G, Shoelson SE, Pant N, Cowburn D. Kuriyan J. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures, of the complexed and peptide-free forms. Cell 72:779-90
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 114
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the amino-terminal SH2 domain of the SYP tyrosine phosphatase
    • Lee CH, Kominos D, Jacques S, Margolis B, Schlessinger J, et al. 1994. Crystal structures of peptide complexes of the amino-terminal SH2 domain of the SYP tyrosine phosphatase. Structure 2:423-38
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.H.1    Kominos, D.2    Jacques, S.3    Margolis, B.4    Schlessinger, J.5
  • 115
    • 0026601293 scopus 로고
    • Point mutations in the ab1 SH2 domain coordinately impair phosphotyrosine binding in vitro and trandforming activity in vivo
    • Mayer BJ, Jackson PK, Van Etten RA, Baltimore D. 1992. Point mutations in the ab1 SH2 domain coordinately impair phosphotyrosine binding in vitro and trandforming activity in vivo. Mol. Cell. Biol. 12:609-18
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    Van Etten, R.A.3    Baltimore, D.4
  • 116
    • 0026085468 scopus 로고
    • A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine
    • Escobedo JA, Kaplan DR, Kavanaugh WM, Turck CW, Williams LT. 1991. A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine. Mol. Cell. Biol. 11:1125-32
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1125-1132
    • Escobedo, J.A.1    Kaplan, D.R.2    Kavanaugh, W.M.3    Turck, C.W.4    Williams, L.T.5
  • 117
    • 0026652899 scopus 로고
    • Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signalling pathways
    • Fantl WJ, Escobedo JA, Martin GA, et al. 1992. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signalling pathways. Cell 69:413-23
    • (1992) Cell , vol.69 , pp. 413-423
    • Fantl, W.J.1    Escobedo, J.A.2    Martin, G.A.3
  • 120
    • 0027219258 scopus 로고
    • A novel recognition motif for phosphatidylinositol 3-kinase binding mediates its association with the hepatocyte growth factor/scatter factor receptor
    • Ponzetto C, Bardelli A, Maina F, Longati P, Panayotou G, et al. 1993. Mol. Cell. Biol. A novel recognition motif for phosphatidylinositol 3-kinase binding mediates its association with the hepatocyte growth factor/scatter factor receptor. 13:4600-8
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4600-4608
    • Ponzetto, C.1    Bardelli, A.2    Maina, F.3    Longati, P.4    Panayotou, G.5
  • 121
    • 0027521783 scopus 로고
    • Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor
    • Nishimura R, Li W, Kashishian A, Mondino A, Shou M, et al. 1993. Mol. Cell. Biol. Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor. 13:6889-96
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6889-6896
    • Nishimura, R.1    Li, W.2    Kashishian, A.3    Mondino, A.4    Shou, M.5
  • 122
    • 0028351702 scopus 로고
    • A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family
    • Ponzetto C, Bardelli A. Zhen Z, Maina F, Zonca PD, et al. 1994. A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family. Cell 77:261-71
    • (1994) Cell , vol.77 , pp. 261-271
    • Ponzetto, C.1    Bardelli, A.2    Zhen, Z.3    Maina, F.4    Zonca, P.D.5
  • 123
    • 0028277954 scopus 로고
    • Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins
    • Soler C, Beguino L, Carpenter G. 1994. Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins. J. Biol. Chem. 269:12320-24
    • (1994) J. Biol. Chem. , vol.269 , pp. 12320-12324
    • Soler, C.1    Beguino, L.2    Carpenter, G.3
  • 124
    • 0026660653 scopus 로고
    • The phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation
    • Backer JM, Myers MG Jr, Shoelson SE, Chin DJ, Sun X, et al. 1992. The phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J. 11:3469-79
    • (1992) EMBO J. , vol.11 , pp. 3469-3479
    • Backer, J.M.1    Myers Jr., M.G.2    Shoelson, S.E.3    Chin, D.J.4    Sun, X.5
  • 125
    • 0026489451 scopus 로고
    • IRS-1 activates the phosphatidylinositol 3′-kinase by associating with the src homolog y 2 domains of p85
    • Myers MG Jr, Backer JM, Sun XJ, Shoelson SE, Hu P, et al. 1992. IRS-1 activates the phosphatidylinositol 3′-kinase by associating with the src homolog y 2 domains of p85. Proc. Natl. Acad. Sci. USA 89:10350-54
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10350-10354
    • Myers Jr., M.G.1    Backer, J.M.2    Sun, X.J.3    Shoelson, S.E.4    Hu, P.5
  • 126
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller R, Cantley LC. 1994. Phosphatidylinositol 3-kinase. BioEssays 16: 565-76
    • (1994) BioEssays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 129
    • 0026720350 scopus 로고
    • Phosphatidylinositol 3-kinase: Structure and expression of the 110 kDa catalytic subunit
    • Hiles ID, Otsu M, Volina S, Fry MJ. Gout I, et al. 1992. Phosphatidylinositol 3-kinase: structure and expression of the 110 kDa catalytic subunit. Cell 70:419-29
    • (1992) Cell , vol.70 , pp. 419-429
    • Hiles, I.D.1    Otsu, M.2    Volina, S.3    Fry, M.J.4    Gout, I.5
  • 130
    • 0027361002 scopus 로고
    • Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85
    • Hu P, Mondino A, Skolnik EY, Schlessinger J. 1993. Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol. Cell. Biol. 13:7677-88
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7677-7688
    • Hu, P.1    Mondino, A.2    Skolnik, E.Y.3    Schlessinger, J.4
  • 131
    • 0027212268 scopus 로고
    • The new elements in insulin signaling. Insulin receptor substrate-1 and proteins with SH2 domains
    • Myers MG Jr, White MF. 1993. The new elements in insulin signaling. Insulin receptor substrate-1 and proteins with SH2 domains. Diabetes 42:643-50
    • (1993) Diabetes , vol.42 , pp. 643-650
    • Myers Jr., M.G.1    White, M.F.2
  • 132
    • 0028157767 scopus 로고
    • PI3-kinase: Structural and functional analysis of intersubunit interactions
    • Dhand R, Hara K, Hiles I, Bax B, Gout I, et al. 1994. PI3-kinase: structural and functional analysis of intersubunit interactions. EMBO J. 13:511-21
    • (1994) EMBO J. , vol.13 , pp. 511-521
    • Dhand, R.1    Hara, K.2    Hiles, I.3    Bax, B.4    Gout, I.5
  • 133
    • 0028178428 scopus 로고
    • Direct association of p110-beta phosphatidylinositol 3-kinase with p85 is mediated by an n-terminal fragment of p110-beta
    • Hu P, Schlessinger J. 1994. Direct association of p110-beta phosphatidylinositol 3-kinase with p85 is mediated by an n-terminal fragment of p110-beta. Mol. Cell. Biol. 14:2577-83
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2577-2583
    • Hu, P.1    Schlessinger, J.2
  • 134
    • 9344254327 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 135
    • 0028120902 scopus 로고
    • Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p 110 and p85 sub units
    • Holt KH, Olson L, Moye Rowley WS, Pessin JE. 1994. Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p 110 and p85 sub units. Mol. Cell. Biol. 14:42-49
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 42-49
    • Holt, K.H.1    Olson, L.2    Moye Rowley, W.S.3    Pessin, J.E.4
  • 136
    • 0027193980 scopus 로고
    • Divergent regulation of phosphatidylinositol 3-kinase P85αa and P85β isoforms upon T cell activation
    • Reif K, Gout I, Waterfield MD, Cantrell DA. 1993. Divergent regulation of phosphatidylinositol 3-kinase P85αa and P85β isoforms upon T cell activation. J. Biol. Chem. 268:10780-88
    • (1993) J. Biol. Chem. , vol.268 , pp. 10780-10788
    • Reif, K.1    Gout, I.2    Waterfield, M.D.3    Cantrell, D.A.4
  • 137
    • 0028152517 scopus 로고
    • Regulation by insulin of phosphatidylinositol 3′-kinase bound to α- and β-Isoforms of p85 regulatory subunit
    • Baltensperger K, Kozma LM, Jaspers SR, Czech MP. 1994. Regulation by insulin of phosphatidylinositol 3′-kinase bound to α- and β-Isoforms of p85 regulatory subunit. J. Biol. Chem. 269: 28937-46
    • (1994) J. Biol. Chem. , vol.269 , pp. 28937-28946
    • Baltensperger, K.1    Kozma, L.M.2    Jaspers, S.R.3    Czech, M.P.4
  • 138
    • 0026315717 scopus 로고
    • Impaired expression of glycogen synthase mRNA in skeletal muscle of NIDDM patients
    • Vesterguard H, Anderson PH, Bak JF, Pederson O. 1991. Impaired expression of glycogen synthase mRNA in skeletal muscle of NIDDM patients. Diabetes 40:1740-45
    • (1991) Diabetes , vol.40 , pp. 1740-1745
    • Vesterguard, H.1    Anderson, P.H.2    Bak, J.F.3    Pederson, O.4
  • 139
    • 0027412618 scopus 로고
    • Insulin-stimulated phosphatidylinositol 3-kinase: Association with a 185-kDa tyrosine-phosphorylated protein (IRS-1 ) and localization in a low density membrane vesicle
    • Kelly KL, Ruderman NB. 1993. Insulin-stimulated phosphatidylinositol 3-kinase: association with a 185-kDa tyrosine-phosphorylated protein (IRS-1 ) and localization in a low density membrane vesicle. J. Biol. Chem. 268:4391-98
    • (1993) J. Biol. Chem. , vol.268 , pp. 4391-4398
    • Kelly, K.L.1    Ruderman, N.B.2
  • 141
    • 0027416751 scopus 로고
    • Association of IRS-I with the insulin receptor and the phosphatidylinositol 3′-kinase. Formation of binary and ternary signaling complexes in intact cells
    • Backer JM, Myers MG Jr, Sun XJ, Chin DJ. Shoelson SE, et al. 1993. Association of IRS-I with the insulin receptor and the phosphatidylinositol 3′-kinase. Formation of binary and ternary signaling complexes in intact cells. J. Biol. Chem. 268:8204-12
    • (1993) J. Biol. Chem. , vol.268 , pp. 8204-8212
    • Backer, J.M.1    Myers Jr., M.G.2    Sun, X.J.3    Chin, D.J.4    Shoelson, S.E.5
  • 142
    • 0028012445 scopus 로고
    • Direct activation of the phospbatidylinositol 3′-kinase by the insulin receptor
    • Van Horn DJ, Myers MG Jr, Backer JM. 1994. Direct activation of the phospbatidylinositol 3′-kinase by the insulin receptor. J. Biochem. 269:29-32
    • (1994) J. Biochem. , vol.269 , pp. 29-32
    • Van Horn, D.J.1    Myers Jr., M.G.2    Backer, J.M.3
  • 143
    • 0028909206 scopus 로고
    • Regulation of phosphatidylinositol 3-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85 kDa regulatory subunit
    • Rordorf-Nikolic T, Van Horn DJ, Chen D, White MF, Backer JM. 1995. Regulation of phosphatidylinositol 3-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85 kDa regulatory subunit. J. Biol. Chem. 270:3662-66
    • (1995) J. Biol. Chem. , vol.270 , pp. 3662-3666
    • Rordorf-Nikolic, T.1    Van Horn, D.J.2    Chen, D.3    White, M.F.4    Backer, J.M.5
  • 145
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu Q, Klippel A, Muslin AJ, Fand WJ. Williams LT. 1995. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 268:100
    • (1995) Science , vol.268 , pp. 100
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fand, W.J.4    Williams, L.T.5
  • 146
    • 0026523559 scopus 로고
    • Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK
    • Wood KW, Sarnecki C, Roberts TM, Blenis J. 1992. ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK. Cell 68: 1041-50
    • (1992) Cell , vol.68 , pp. 1041-1050
    • Wood, K.W.1    Sarnecki, C.2    Roberts, T.M.3    Blenis, J.4
  • 147
    • 0028178928 scopus 로고
    • PDGF-and insulin-dependent pp70S6k activation mediated by phosphatidylinositol3-OH kinase
    • Chung J, Grammer TC, Lemon KP, Kazlauskas A, Blenis J. 1994. PDGF-and insulin-dependent pp70S6k activation mediated by phosphatidylinositol3-OH kinase. Nature 370:71-75
    • (1994) Nature , vol.370 , pp. 71-75
    • Chung, J.1    Grammer, T.C.2    Lemon, K.P.3    Kazlauskas, A.4    Blenis, J.5
  • 148
    • 0027981333 scopus 로고
    • 1-Phosphatidylinositol 3-kinase activity is required for insulin-stimulated glucose transport but not for ras activation in CHO cells
    • Hara K, Yonezawa K, Sakaue H, Ando A, Kotani K, et al. 1994. 1-Phosphatidylinositol 3-kinase activity is required for insulin-stimulated glucose transport but not for ras activation in CHO cells. Proc. Natl. Acad. Sci. USA 91:7415-19
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7415-7419
    • Hara, K.1    Yonezawa, K.2    Sakaue, H.3    Ando, A.4    Kotani, K.5
  • 149
    • 0029009331 scopus 로고
    • Ras-independent and wortmannin-sensitive activation of glycogen synthase by insulin in Chinese Hamster Ovary Cells
    • Sakaue H, Hara K, Noguchi T, Matozaki T. Kotani K, et al. 1995. Ras-independent and wortmannin-sensitive activation of glycogen synthase by insulin in Chinese Hamster Ovary Cells. J. Biol. Chem. 270:11304-9
    • (1995) J. Biol. Chem. , vol.270 , pp. 11304-11309
    • Sakaue, H.1    Hara, K.2    Noguchi, T.3    Matozaki, T.4    Kotani, K.5
  • 150
    • 0028308412 scopus 로고
    • Phosphatidylinositol 3-kinase activation is requried for insulin stimulation of pp70 S6 kinase, DNA synthesis and glucose tranporter translocation
    • Cheatham B, Vlahos CJ, Cheatham L, Wang L, Blenis J, Kahn CR. 1994. Phosphatidylinositol 3-kinase activation is requried for insulin stimulation of pp70 S6 kinase, DNA synthesis and glucose tranporter translocation. Mol. Cell. Biol. 14:4902-11
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4902-4911
    • Cheatham, B.1    Vlahos, C.J.2    Cheatham, L.3    Wang, L.4    Blenis, J.5    Kahn, C.R.6
  • 151
    • 0029090212 scopus 로고
    • Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase
    • Stoyanov S, Volinia S, Hanck T, Rubio I, Loubtchenkov M, et al. 1995. Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase. Science 269:690-93
    • (1995) Science , vol.269 , pp. 690-693
    • Stoyanov, S.1    Volinia, S.2    Hanck, T.3    Rubio, I.4    Loubtchenkov, M.5
  • 152
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein β-gamma subunits
    • Stephens L, Smrcka A, Cooke FT, Jackson TR, Sternweis PC, Hawkins PT. 1994. A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein β-gamma subunits. Cell 77:83-93
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 153
    • 0029057336 scopus 로고
    • A single ataxia telangectasia gene with a product similar to PI 3-kinase
    • Savitsky K, Bar-Shira A, Gilad S, Rotman G, Ziv Y, et al. 1995. A single ataxia telangectasia gene with a product similar to PI 3-kinase. Science 268: 1749-53
    • (1995) Science , vol.268 , pp. 1749-1753
    • Savitsky, K.1    Bar-Shira, A.2    Gilad, S.3    Rotman, G.4    Ziv, Y.5
  • 154
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VOS34 gene is essential for protein sorting
    • Schu PV, Kaoru T, Fry MJ, Stack JH, Waterfield MD, Emr SD. 1993. Phosphatidylinositol 3-kinase encoded by yeast VOS34 gene is essential for protein sorting. Science 26:88-91
    • (1993) Science , vol.26 , pp. 88-91
    • Schu, P.V.1    Kaoru, T.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 155
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
    • Stack JH, Herman PK, Schu PV, Emr SD. 1993. A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J. 12: 2195-204
    • (1993) EMBO J. , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 156
    • 0028981018 scopus 로고
    • A human phosphatidylinositol 3-kinase complex related to the yeast ps34p-Vps15p protein sorting system
    • Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, et al. 1995. A human phosphatidylinositol 3-kinase complex related to the yeast ps34p-Vps15p protein sorting system. EMBO J. 14:3339-48
    • (1995) EMBO J. , vol.14 , pp. 3339-3348
    • Volinia, S.1    Dhand, R.2    Vanhaesebroeck, B.3    MacDougall, L.K.4    Stein, R.5
  • 158
    • 0028598672 scopus 로고
    • RAPT 1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex
    • Chiu MI, Katz H, Berlin V. 1994. RAPT 1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex. Proc. Natl. Acad. Sci. USA 91:12574-78
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12574-12578
    • Chiu, M.I.1    Katz, H.2    Berlin, V.3
  • 159
    • 0028239893 scopus 로고
    • RAFTI1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • Sabatini DM, Erdjument-Bromage H, Lui M, Tempst P, Snyder SH. 1994. RAFTI1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78:35-43
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 160
    • 0027382875 scopus 로고
    • Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity
    • Cafferkey R, Young PR, McLaughlin MM, Bergsma DJ, Koltin Y, et al. 1993. Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity. Mol. Cell. Biol. 13:6012-22
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6012-6022
    • Cafferkey, R.1    Young, P.R.2    McLaughlin, M.M.3    Bergsma, D.J.4    Koltin, Y.5
  • 162
    • 0029058288 scopus 로고
    • Phosphatidylinositol 3-kinase activity is required at a postendocytic step in platelet-derived growth factor receptor trafficking
    • Joly M, Kazlauskas A, Corvera S. 1995. Phosphatidylinositol 3-kinase activity is required at a postendocytic step in platelet-derived growth factor receptor trafficking. J. Biol. Chem. 270:13225-30
    • (1995) J. Biol. Chem. , vol.270 , pp. 13225-13230
    • Joly, M.1    Kazlauskas, A.2    Corvera, S.3
  • 163
    • 0028351218 scopus 로고
    • Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites
    • Joly M, Kazlauskas A, Fay FS, Corvera S. 1994. Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites. Science 263:684-87
    • (1994) Science , vol.263 , pp. 684-687
    • Joly, M.1    Kazlauskas, A.2    Fay, F.S.3    Corvera, S.4
  • 164
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel mositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman M, Downes CP, Keeler M, Keller T, Cantley L. 1988. Type I phosphatidylinositol kinase makes a novel mositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332:644-46
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 165
    • 0027535742 scopus 로고
    • Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi H, Brewer KA, Exton JH. 1993. Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 268: 13-16
    • (1993) J. Biol. Chem. , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 167
    • 0027496054 scopus 로고
    • Metabolic origin of insulin resistance in obesity with and without Type II diabetes mellitus
    • Felber JD, Haesler E, Jequier E. 1993. Metabolic origin of insulin resistance in obesity with and without Type II diabetes mellitus. Diabetologia 36:1221-29
    • (1993) Diabetologia , vol.36 , pp. 1221-1229
    • Felber, J.D.1    Haesler, E.2    Jequier, E.3
  • 169
    • 0027953284 scopus 로고
    • PI-3-kinase is a dual specificity enzyme - Autoregulation by an intrinsic protein-serine kinase activity
    • Dhand R, Hiles I, Panayotou G, Roche S, Fry MJ, et al. 1994. PI-3-kinase is a dual specificity enzyme - autoregulation by an intrinsic protein-serine kinase activity. EMBO J. 13:522-33
    • (1994) EMBO J. , vol.13 , pp. 522-533
    • Dhand, R.1    Hiles, I.2    Panayotou, G.3    Roche, S.4    Fry, M.J.5
  • 171
    • 0027211693 scopus 로고
    • Phospholipase C-gammal and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • Valius M, Kazlauskas A. 1993. Phospholipase C-gammal and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell 73:321-34
    • (1993) Cell , vol.73 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 172
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adcock M, Fernley R, Wade J, Pawson T, Bowtell D. 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature 363:83-85
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 173
    • 0027312272 scopus 로고
    • Guanine-nucleotide-releasing factor mSos1 binds to Grb2 and links receptor tyrosine kinases to ras signalling
    • Li N, Batzer A, Daly R, Yajnik V, Skolnik E, et al. 1993. Guanine-nucleotide-releasing factor mSos1 binds to Grb2 and links receptor tyrosine kinases to ras signalling. Nature 363:85-88
    • (1993) Nature , vol.363 , pp. 85-88
    • Li, N.1    Batzer, A.2    Daly, R.3    Yajnik, V.4    Skolnik, E.5
  • 174
    • 0027910431 scopus 로고
    • Association of Sos ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan SE, Giddings BW, Brooks MW, Buday L, Sizeland AM, Weinberg RA. 1993. Association of Sos ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 363:45-51
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 175
    • 0027117408 scopus 로고
    • A signal chain of events
    • Roberts TM. 1992. A signal chain of events. Nature 360:534-35
    • (1992) Nature , vol.360 , pp. 534-535
    • Roberts, T.M.1
  • 176
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing proteins GRB 2 links receptor tyrosine kinases to ras signaling
    • Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, et al. 1992. The SH2 and SH3 domain-containing proteins GRB 2 links receptor tyrosine kinases to ras signaling. Cell 70:431-42
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3    Li, W.4    Margolis, B.5
  • 177
    • 0028342948 scopus 로고
    • SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor β-receptor, epidermal growth factor receptor, and insulin receptor substrate-1-derived phosphopeptides
    • Case RD, Piccione E, Wolf G, Benett AM, Lechleider RJ, et al. 1994. SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor β-receptor, epidermal growth factor receptor, and insulin receptor substrate-1-derived phosphopeptides. J. Biol. Chem. 269:10467-74
    • (1994) J. Biol. Chem. , vol.269 , pp. 10467-10474
    • Case, R.D.1    Piccione, E.2    Wolf, G.3    Benett, A.M.4    Lechleider, R.J.5
  • 178
    • 0027490590 scopus 로고
    • Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SHPTP2
    • Lechleider RJ, Freeman RM, Neel BG. 1993. Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SHPTP2. J Biol. Chem. 268:13434-38
    • (1993) J Biol. Chem. , vol.268 , pp. 13434-13438
    • Lechleider, R.J.1    Freeman, R.M.2    Neel, B.G.3
  • 179
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor B
    • Lechleider RJ, Sugimoto S, Bennett AM, Kashishian AS, Cooper JA, et al. 1993. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor B. J. Biol. Chem. 268:21478-81
    • (1993) J. Biol. Chem. , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5
  • 180
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase: A putative homolog of Drosophila corkscrew
    • Freeman RM, Plutzky J, Neel BG. 1992. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc. Natl. Acad. Sci. USA 89:11239-43
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11239-11243
    • Freeman, R.M.1    Plutzky, J.2    Neel, B.G.3
  • 182
    • 0029065980 scopus 로고
    • Different signaling roles of SHPTP2 in insulin-induced GLUT1 expression and GLUT4 translocation
    • Hausdorff SF, Bennett AM, Neel BG, Birnbaum MJ. 1995. Different signaling roles of SHPTP2 in insulin-induced GLUT1 expression and GLUT4 translocation. J. Biol. Chem. 270:12965-68
    • (1995) J. Biol. Chem. , vol.270 , pp. 12965-12968
    • Hausdorff, S.F.1    Bennett, A.M.2    Neel, B.G.3    Birnbaum, M.J.4
  • 183
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated ras activation
    • Noguchi T, Matozaki T, Horita K, Fujioka Y, Kasuga M. 1994. Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated ras activation. Mol. Cell. Biol. 14:6674-82
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 184
    • 0028136280 scopus 로고
    • Expression of catalytically inactive syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin
    • Milarski KL, Saltiel AR. 1995. Expression of catalytically inactive syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin. J. Biol. Chem. 269:21239-43
    • (1995) J. Biol. Chem. , vol.269 , pp. 21239-21243
    • Milarski, K.L.1    Saltiel, A.R.2
  • 185
    • 0028896991 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling
    • Yamauchi K, Milarski KL, Saltiel AR, Pessin JE. 1995. Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc. Natl. Acad. Sci. USA 92:664-68
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 664-668
    • Yamauchi, K.1    Milarski, K.L.2    Saltiel, A.R.3    Pessin, J.E.4
  • 187
    • 0027939555 scopus 로고
    • Signal transduction pathways from insulin receptor to ras-analysis by mutant insulin receptors
    • Yonezawa K, Ando A, Kaburagi Y, Yamamotohonda R, Kitamura T, et al. 1994. Signal transduction pathways from insulin receptor to ras-analysis by mutant insulin receptors. J. Biol. Chem. 269:4634-40
    • (1994) J. Biol. Chem. , vol.269 , pp. 4634-4640
    • Yonezawa, K.1    Ando, A.2    Kaburagi, Y.3    Yamamotohonda, R.4    Kitamura, T.5
  • 188
    • 0028341446 scopus 로고
    • Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras formation
    • 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 formation. J. Biol. Chem. 269: 10734-38
    • (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
  • 189
    • 0028036795 scopus 로고
    • Localization of the insulin receptor binding sites for the SH2 domain proteins p85, syp, and GAP
    • Staubs PA, Reichart DR, Saltiel AR, Milarski KL, Maegawa H, et al. 1994. Localization of the insulin receptor binding sites for the SH2 domain proteins p85, syp, and GAP. J. Biol. Chem. 269:27186-92
    • (1994) J. Biol. Chem. , vol.269 , pp. 27186-27192
    • Staubs, P.A.1    Reichart, D.R.2    Saltiel, A.R.3    Milarski, K.L.4    Maegawa, H.5
  • 190
    • 0028342629 scopus 로고
    • 538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains
    • 538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains. J. Biol. Chem. 269:12220-28
    • (1994) J. Biol. Chem. , vol.269 , pp. 12220-12228
    • Uchida, T.1    Matozaki, T.2    Noguchi, T.3    Yamao, T.4    Horita, K.5
  • 191
    • 0029038910 scopus 로고
    • Association of insulin receptor substrate 1 with simian virus 40 large T antigen
    • Zhou-Li F, D'Ambrosio C, Li S, Surmacz E, Baserga R. 1995. Association of insulin receptor substrate 1 with simian virus 40 large T antigen. Mol. Cell. BioL 15:4232-39
    • (1995) Mol. Cell. BioL , vol.15 , pp. 4232-4239
    • Zhou-Li, F.1    D'Ambrosio, C.2    Li, S.3    Surmacz, E.4    Baserga, R.5
  • 192
    • 0027964728 scopus 로고
    • Synergistic activation by Ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator
    • Shimizu K, Kuroda S, Yamamori B, Matsuda S, Kaibuchi K, et al. 1994. Synergistic activation by Ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator. J. Biol. Chem. 269:22917-20
    • (1994) J. Biol. Chem. , vol.269 , pp. 22917-22920
    • Shimizu, K.1    Kuroda, S.2    Yamamori, B.3    Matsuda, S.4    Kaibuchi, K.5
  • 193
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed E, Symons M, Macdonald SG, McCormick F, Ruggieri R. 1994. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265:1713-16
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 194
    • 0028051904 scopus 로고
    • Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
    • Irie K, Gotoh Y, Yashar BM, Errede B, Nishida E, Matsumoto K. 1994. Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 265:1716-19
    • (1994) Science , vol.265 , pp. 1716-1719
    • Irie, K.1    Gotoh, Y.2    Yashar, B.M.3    Errede, B.4    Nishida, E.5    Matsumoto, K.6
  • 195
    • 0028115999 scopus 로고
    • Interaction of the protein kinase Raf-1 with 14-3-3 proteins
    • Fu H, Xia K, Pallas DC, Cui C, Conroy K, et al. 1994. Interaction of the protein kinase Raf-1 with 14-3-3 proteins [see comments]. Science 266:126-29
    • (1994) Science , vol.266 , pp. 126-129
    • Fu, H.1    Xia, K.2    Pallas, D.C.3    Cui, C.4    Conroy, K.5
  • 197
    • 0028052219 scopus 로고
    • Activation of protein kinase C by purified bovine brain 14-3-3: Comparison with tyrosine hydroxylase activation
    • Tanji M, Horwitz R, Rosenfeld G, Waymire JC. 1994. Activation of protein kinase C by purified bovine brain 14-3-3: comparison with tyrosine hydroxylase activation. J. Neurochem. 63: 1908-16
    • (1994) J. Neurochem. , vol.63 , pp. 1908-1916
    • Tanji, M.1    Horwitz, R.2    Rosenfeld, G.3    Waymire, J.C.4
  • 199
    • 0028335858 scopus 로고
    • Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex
    • Du X, Harris SJ, Tetaz TJ, Ginsberg MH, Berndt MC. 1994. Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex. J. Biol. Chem. 269:18287-90
    • (1994) J. Biol. Chem. , vol.269 , pp. 18287-18290
    • Du, X.1    Harris, S.J.2    Tetaz, T.J.3    Ginsberg, M.H.4    Berndt, M.C.5
  • 200
    • 0028241170 scopus 로고
    • 14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation
    • Chen F, Wagner PD. 1994. 14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation. FEBS Lett. 347:128-32
    • (1994) FEBS Lett. , vol.347 , pp. 128-132
    • Chen, F.1    Wagner, P.D.2
  • 201
    • 0028270296 scopus 로고
    • Mechanism of inhibition of protein kinase C by 14-3-3 isoforms. 14-3-3 isoforms do not have phospholipase A2 activity
    • Robinson K, Jones D, Patel Y, Martin H, Madrazo J, et al. 1994. Mechanism of inhibition of protein kinase C by 14-3-3 isoforms. 14-3-3 isoforms do not have phospholipase A2 activity. Biochem. J. 299:853-61
    • (1994) Biochem. J. , vol.299 , pp. 853-861
    • Robinson, K.1    Jones, D.2    Patel, Y.3    Martin, H.4    Madrazo, J.5
  • 202
    • 0027201574 scopus 로고
    • Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein
    • Furukawa Y, Ikuta N, Omata S, Yamauchi T, Isobe T, Ichimura T. 1993. Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein. Biochem. Biophys. Res. Commun. 194: 144-49
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 144-149
    • Furukawa, Y.1    Ikuta, N.2    Omata, S.3    Yamauchi, T.4    Isobe, T.5    Ichimura, T.6
  • 205
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
    • Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, et al. 1995. Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 376:188-91
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3    Dodson, G.G.4    Soneji, Y.5
  • 207
    • 0028641601 scopus 로고
    • Association of insulin receptor substrate-1 with integrins
    • Vuori K, Ruoslahti E. 1994. Association of insulin receptor substrate-1 with integrins. Science 266:1576-78
    • (1994) Science , vol.266 , pp. 1576-1578
    • Vuori, K.1    Ruoslahti, E.2
  • 208
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233-39
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 209
    • 0028032895 scopus 로고
    • Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene
    • Araki E, Lipes MA, Patti ME, Bruning JC, Haag B III, et al. 1994. Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene. Nature 372:186-90
    • (1994) Nature , vol.372 , pp. 186-190
    • Araki, E.1    Lipes, M.A.2    Patti, M.E.3    Bruning, J.C.4    Haag III, B.5
  • 210
    • 0028032894 scopus 로고
    • Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1
    • Tamemoto H, Kadowaki T, Tobe K, Tobe K, Yagi T, Sakura H, et al. 1994. Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1. Nature 372:182-86
    • (1994) Nature , vol.372 , pp. 182-186
    • Tamemoto, H.1    Kadowaki, T.2    Tobe, K.3    Tobe, K.4    Yagi, T.5    Sakura, H.6
  • 211
    • 0028226039 scopus 로고
    • Enhancement or inhibition of insulin signaling by insulin receptor substrate 1 is cell context dependent
    • Yamauchi K, Pessin JE. 1994. Enhancement or inhibition of insulin signaling by insulin receptor substrate 1 is cell context dependent. Mol. Cell. Biol. 14: 4427-34
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4427-4434
    • Yamauchi, K.1    Pessin, J.E.2
  • 213
    • 0027451389 scopus 로고
    • Functional expression of insulin receptor substrate-1 is required for insulin-stimulated mitogenic signaling
    • Waters SB, Yamauchi K, Pessin JE. 1993. Functional expression of insulin receptor substrate-1 is required for insulin-stimulated mitogenic signaling. J. Biol. Chem. 238:22231-34
    • (1993) J. Biol. Chem. , vol.238 , pp. 22231-22234
    • Waters, S.B.1    Yamauchi, K.2    Pessin, J.E.3
  • 214
    • 0026607990 scopus 로고
    • Mammalian facilitative glucose transporter family: Structure and molecular regulation
    • Pessin JE, Bell GI. 1992. Mammalian facilitative glucose transporter family: structure and molecular regulation. Annu. Rev. Physiol. 54:911-30
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 911-930
    • Pessin, J.E.1    Bell, G.I.2
  • 216
    • 0028124189 scopus 로고
    • Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes
    • Okada T, Kawano Y, Sakakibara T, Hazeki O, Ui M. 1994. Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes. J. Biochem. 269:3568-73
    • (1994) J. Biochem. , vol.269 , pp. 3568-3573
    • Okada, T.1    Kawano, Y.2    Sakakibara, T.3    Hazeki, O.4    Ui, M.5
  • 217
    • 0027930436 scopus 로고
    • PI-3-tanase inhibitor wortmannin blocks the insulin-like effects of growth hormone in isolated rat adipocytes
    • Ridderstrale M, Tornqvist H. 1994. PI-3-tanase inhibitor wortmannin blocks the insulin-like effects of growth hormone in isolated rat adipocytes. Biochem. Biophys. Res. Commun. 203: 306-10
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 306-310
    • Ridderstrale, M.1    Tornqvist, H.2
  • 218
    • 0028124189 scopus 로고
    • Essential role of phsophatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes-studies with a selective inhibitor wortmannin
    • Okada T, Kawano Y, Sakakibara T, Hazeki O, Ui M. 1994. Essential role of phsophatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes-studies with a selective inhibitor wortmannin. J. Biol. Chem. 269:3568-73
    • (1994) J. Biol. Chem. , vol.269 , pp. 3568-3573
    • Okada, T.1    Kawano, Y.2    Sakakibara, T.3    Hazeki, O.4    Ui, M.5
  • 219
    • 0028226008 scopus 로고
    • A role for raf-1 in the divergent signaling pathways mediating insulin-stimulated glucose transport
    • Fingar DC, Birnbaum MJ. 1994. A role for raf-1 in the divergent signaling pathways mediating insulin-stimulated glucose transport. J. Biol. Chem. 269: 10127-32
    • (1994) J. Biol. Chem. , vol.269 , pp. 10127-10132
    • Fingar, D.C.1    Birnbaum, M.J.2
  • 220
    • 0027286331 scopus 로고
    • Hormonal/metabolic regulation of the human GLUT4/muscle-fat facilitative glucose transporter gene in transgenic mice
    • Olson AL, Liu ML, Moye-Rowley WS, Buse JB, Bell GI, Pessin JE. 1993. Hormonal/metabolic regulation of the human GLUT4/muscle-fat facilitative glucose transporter gene in transgenic mice. J. Biol. Chem. 268:9839-46
    • (1993) J. Biol. Chem. , vol.268 , pp. 9839-9846
    • Olson, A.L.1    Liu, M.L.2    Moye-Rowley, W.S.3    Buse, J.B.4    Bell, G.I.5    Pessin, J.E.6
  • 221
    • 0028168827 scopus 로고
    • Role of p21ras in insulin-stimulated glucose transport in 3T3-L1 adipocytes
    • Hausdorff SF, Frangioni JV, Birnbaum MJ. 1994. Role of p21ras in insulin-stimulated glucose transport in 3T3-L1 adipocytes. J. Biol. Chem. 269:21391-94
    • (1994) J. Biol. Chem. , vol.269 , pp. 21391-21394
    • Hausdorff, S.F.1    Frangioni, J.V.2    Birnbaum, M.J.3
  • 222
    • 0028114771 scopus 로고
    • Turned on by insulin
    • Proud CG. 1994. Turned on by insulin. Nature 371:747-48
    • (1994) Nature , vol.371 , pp. 747-748
    • Proud, C.G.1
  • 223
    • 0028034140 scopus 로고
    • Missing link in insulin's path to protein production
    • O'Brien C. 1994. Missing link in insulin's path to protein production. Science 266:542-43
    • (1994) Science , vol.266 , pp. 542-543
    • O'Brien, C.1
  • 224
    • 0028222129 scopus 로고
    • Molecular cloning and tissue disuibution of PHAS-I, an intracellular target for insulin and growth factors
    • Hu C, Pang S, Kong X, Velleca M, Lawrence JC. 1994. Molecular cloning and tissue disuibution of PHAS-I, an intracellular target for insulin and growth factors. Proc. Natl. Acad. Sci. USA 91:3730-34
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3730-3734
    • Hu, C.1    Pang, S.2    Kong, X.3    Velleca, M.4    Lawrence, J.C.5
  • 225
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause A, Belsham GJ, Gingras A, Donze O, Lin T, et al. 1994. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371:762-67
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.3    Donze, O.4    Lin, T.5
  • 226
    • 0028126506 scopus 로고
    • PHAS-1 as a link, between mitogen-activated protein kinase and translation initiation
    • Lin TA, Kong XM, Haystead TAJ, Pause A, Belsham G, et al. 1994. PHAS-1 as a link, between mitogen-activated protein kinase and translation initiation. Science 266:653-56
    • (1994) Science , vol.266 , pp. 653-656
    • Lin, T.A.1    Kong, X.M.2    Haystead, T.A.J.3    Pause, A.4    Belsham, G.5
  • 227
    • 0029120591 scopus 로고
    • cAMP-and rapamycin-sensitjve regulation of the association of eukaryotic initiation factor 4E and the translational regulator PHAS-1 in aortic smooth muscle cells
    • Graves LM, Bornfeldt KE, Argast GM, Krebs EG, Kong X, et al. 1995. cAMP-and rapamycin-sensitjve regulation of the association of eukaryotic initiation factor 4E and the translational regulator PHAS-1 in aortic smooth muscle cells. Proc. Natl. Acad. Sci. USA 92 7222-26
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7222-7226
    • Graves, L.M.1    Bornfeldt, K.E.2    Argast, G.M.3    Krebs, E.G.4    Kong, X.5
  • 229
    • 9344230299 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 230
    • 0028023002 scopus 로고
    • Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling
    • Tanti JF, Gremeaux T, Van Obberghen E, Le Marchand-Brustel Y. 1994. Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling. J. Biol. Chem. 269: 6051-57
    • (1994) J. Biol. Chem. , vol.269 , pp. 6051-6057
    • Tanti, J.F.1    Gremeaux, T.2    Van Obberghen, E.3    Le Marchand-Brustel, Y.4
  • 231
    • 0028031569 scopus 로고
    • Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes. Central role of tumor necrosis factor-alpha
    • Hotamisligil GS, Budavari A, Murray D, Spiegelman BM. 1994. Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes. Central role of tumor necrosis factor-alpha. J. Clin. Invest. 94:1543-49
    • (1994) J. Clin. Invest. , vol.94 , pp. 1543-1549
    • Hotamisligil, G.S.1    Budavari, A.2    Murray, D.3    Spiegelman, B.M.4
  • 232
    • 0027459878 scopus 로고
    • Adipose expression of tumor necrosis factor-α: Direct role in obesity-linked insulin resistance
    • Hotamisligil GS, Shargill NS, Spiegelman BM. 1993. Adipose expression of tumor necrosis factor-α: direct role in obesity-linked insulin resistance. Science 259:87-91
    • (1993) Science , vol.259 , pp. 87-91
    • Hotamisligil, G.S.1    Shargill, N.S.2    Spiegelman, B.M.3
  • 233
    • 0004188835 scopus 로고
    • Philadelphia: Saunders. 3rd ed.
    • DeGroot LJ, ed. 1995. Endocrinology. Philadelphia: Saunders. 3rd ed.
    • (1995) Endocrinology
    • DeGroot, L.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.