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Volumn 20, Issue 5, 2000, Pages 1489-1496

Insulin-like growth factor I-induced degradation of insulin receptor substrate 1 is mediated by the 26S proteasome and blocked by phosphatidylinositol 3'-kinase inhibition

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN RECEPTOR SUBSTRATE 1; PHOSPHATIDYLINOSITOL KINASE; PROTEASOME; SOMATOMEDIN C;

EID: 0033982719     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.5.1489-1496.2000     Document Type: Article
Times cited : (112)

References (66)
  • 1
    • 0030978351 scopus 로고    scopus 로고
    • β-Catenin is a target for the ubiquitin-proteasome pathway
    • Aberle, H., A. Bauer, J. Stappert, A. Kispert, and R. Kemler. 1997. β-Catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 16:3797-3804.
    • (1997) EMBO J. , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 2
    • 0031049438 scopus 로고    scopus 로고
    • Effect of tumor necrosis factor-alpha on the phosphorylation of tyrosine kinase receptors is associated with dynamic alterations in specific protein-tyrosine phosphatases
    • Ahmad, F., and B. J. Goldstein. 1997. Effect of tumor necrosis factor-alpha on the phosphorylation of tyrosine kinase receptors is associated with dynamic alterations in specific protein-tyrosine phosphatases. J. Cell. Biochem. 64:117-127.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 117-127
    • Ahmad, F.1    Goldstein, B.J.2
  • 3
    • 0029096089 scopus 로고
    • Characterization and regulation of the mouse insulin receptor substrate gene promoter
    • Araki, E., B. L. Haag III, K. Matsuda, M. Shichiri, and C. R. Kahn. 1995. Characterization and regulation of the mouse insulin receptor substrate gene promoter. Mol. Endocrinol. 9:1367-1379.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1367-1379
    • Araki, E.1    Haag B.L. III2    Matsuda, K.3    Shichiri, M.4    Kahn, C.R.5
  • 4
    • 0028032895 scopus 로고
    • Alternative pathway of insulin-signaling in mice with targeted disruption of the IRS-1 gene
    • Araki, E., M. A. Lipes, M. Patti, J. C. Bruning, B. Haag III, R. S. Johnson, and C. R. Kahn. 1994. Alternative pathway of insulin-signaling in mice with targeted disruption of the IRS-1 gene. Nature 372:186-190.
    • (1994) Nature , vol.372 , pp. 186-190
    • Araki, E.1    Lipes, M.A.2    Patti, M.3    Bruning, J.C.4    Haag B. III5    Johnson, R.S.6    Kahn, C.R.7
  • 5
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C., P. Sen, K. Hofmann, L. Ma, M. Goebl, J. W. Harper, and S. J. Elledge. 1996. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86:263-274.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 6
    • 0027423419 scopus 로고
    • Role of insulin-like growth factors in embryonic and postnatal growth
    • Baker, J., J. P. Liu, E. J. Robertson, and A. Efstratiadis. 1993. Role of insulin-like growth factors in embryonic and postnatal growth. Cell 75:73-82.
    • (1993) Cell , vol.75 , pp. 73-82
    • Baker, J.1    Liu, J.P.2    Robertson, E.J.3    Efstratiadis, A.4
  • 7
    • 0027186439 scopus 로고
    • Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1
    • Cheatham, B., S. E. Shoelson, K. Yamada, E. Goncalves, and C. R. Kahn. 1993. Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1. Proc. Natl. Acad. Sci. USA 90:7336-7340.
    • (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
  • 9
    • 0031465447 scopus 로고    scopus 로고
    • Modulation of insulin receptor substrate-1 tyrosine phosphorylation and function by mitogen-activated protein kinase
    • De Fea, K., and R. A. Roth. 1997. Modulation of insulin receptor substrate-1 tyrosine phosphorylation and function by mitogen-activated protein kinase. J. Biol. Chem. 272:31400-31406.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31400-31406
    • De Fea, K.1    Roth, R.A.2
  • 10
    • 0030669094 scopus 로고    scopus 로고
    • Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612
    • De Fea, K., and R. A. Roth. 1997. Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612. Biochemistry 36:12939-12947.
    • (1997) Biochemistry , vol.36 , pp. 12939-12947
    • De Fea, K.1    Roth, R.A.2
  • 12
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin: A central role for clasto-lactacystin beta-lactone
    • Dick, L. R., A. A. Cruikshank, L. Grenier, F. D. Melandri, S. L. Nunes, and R. L. Stein. 1996. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone. J. Biol. Chem. 271:7273-7276.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7273-7276
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 13
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • Diehl, J. A., F. Zindy, and C. J. Sherr. 1997. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev. 11:957-972.
    • (1997) Genes Dev. , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 14
    • 0032540498 scopus 로고    scopus 로고
    • The role of protein stability in the cell cycle and cancer
    • Elledge, S. J., and J. W. Harper. 1998. The role of protein stability in the cell cycle and cancer. Biochim. Biophys. Acta 1377:M61-M70.
    • (1998) Biochim. Biophys. Acta , vol.1377
    • Elledge, S.J.1    Harper, J.W.2
  • 15
    • 0003882322 scopus 로고
    • Monoclonal antibody to the type I insulin-like growth factor (IGF-I) receptor blocks IGF-I receptor-mediated DNA synthesis: Clarification of the mitogenic mechanisms of IGF-I and insulin in human skin fibroblasts
    • Flier, J. S., P. Usher, and A. C. Moses. 1986. Monoclonal antibody to the type I insulin-like growth factor (IGF-I) receptor blocks IGF-I receptor-mediated DNA synthesis: clarification of the mitogenic mechanisms of IGF-I and insulin in human skin fibroblasts. Proc. Natl. Acad. Sci. USA 83:664-668.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 664-668
    • Flier, J.S.1    Usher, P.2    Moses, A.C.3
  • 16
    • 0030723979 scopus 로고    scopus 로고
    • Angiotensin II inhibits insulin signaling in aortic smooth muscle cells at multiple levels. A potential role for serine phosphorylation in insulin/angiotensin II crosstalk
    • Folli, F., C. R. Kahn, H. Hansen, J. L. Bouchie, and E. P. Feener. 1997. Angiotensin II inhibits insulin signaling in aortic smooth muscle cells at multiple levels. A potential role for serine phosphorylation in insulin/angiotensin II crosstalk. J. Clin. Investig. 100:2158-2169.
    • (1997) J. Clin. Investig. , vol.100 , pp. 2158-2169
    • Folli, F.1    Kahn, C.R.2    Hansen, H.3    Bouchie, J.L.4    Feener, E.P.5
  • 17
    • 0028979617 scopus 로고
    • The PI3-kinase serine kinase phosphorylates its p85 subunit and IRS-1 in PI3-kinase/IRS-1 complexes
    • Freund, G. G., J. G. Wittig, and R. A. Mooney. 1995. The PI3-kinase serine kinase phosphorylates its p85 subunit and IRS-1 in PI3-kinase/IRS-1 complexes. Biochem. Biophys. Res. Commun. 206:272-278.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 272-278
    • Freund, G.G.1    Wittig, J.G.2    Mooney, R.A.3
  • 18
    • 0027569865 scopus 로고
    • Regulation of insulin receptor signaling by protein-tyrosine dephosphorylation
    • Goldstein, B. J. 1993. Regulation of insulin receptor signaling by protein-tyrosine dephosphorylation. Receptor 3:1-15.
    • (1993) Receptor , vol.3 , pp. 1-15
    • Goldstein, B.J.1
  • 19
    • 0030743040 scopus 로고    scopus 로고
    • Insulin and interleukin-4 induce desensitization to the mitogenic effects of insulin-like growth factor-I. Pivotal role for insulin receptor substrate-2
    • Haddad, T. C., and C. A. Conover. 1997. Insulin and interleukin-4 induce desensitization to the mitogenic effects of insulin-like growth factor-I. Pivotal role for insulin receptor substrate-2. J. Biol. Chem. 272:19525-19531.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19525-19531
    • Haddad, T.C.1    Conover, C.A.2
  • 20
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 21
    • 0025853324 scopus 로고
    • The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo
    • Hochstrasser, M., M. J. Ellison, V. Chau, and A. Varshavsky. 1991. The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo. Proc. Natl. Acad. Sci. USA 88:4606-4610.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4606-4610
    • Hochstrasser, M.1    Ellison, M.J.2    Chau, V.3    Varshavsky, A.4
  • 22
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha-and obesity-induced insulin resistance
    • Hotamisligil, G. S., P. Peraldi, A. Budavari, R. Ellis, M. F. White, and B. M. Spiegelman. 1996. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha-and obesity-induced insulin resistance. Science 271:665-668.
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 23
    • 0029855761 scopus 로고    scopus 로고
    • Different pathways of postreceptor desensitization following chronic insulin treatment and in cells overexpressing constitutively active insulin receptors
    • Inoue, G., B. Cheatham, and C. R. Kahn. 1996. Different pathways of postreceptor desensitization following chronic insulin treatment and in cells overexpressing constitutively active insulin receptors. J. Biol. Chem 271: 28206-28211.
    • (1996) J. Biol. Chem , vol.271 , pp. 28206-28211
    • Inoue, G.1    Cheatham, B.2    Kahn, C.R.3
  • 24
    • 0032540288 scopus 로고    scopus 로고
    • Insulin receptor substrate-1 (IRS-1) is the predominant signaling molecule activated by insulin-like growth factor-I (IGF-I), insulin, and interleukin-4 (IL-4) in estrogen receptor-positive human breast cancer cells
    • Jackson, J. G., M. F. White, and D. Yee. 1998. Insulin receptor substrate-1 (IRS-1) is the predominant signaling molecule activated by insulin-like growth factor-I (IGF-I), insulin, and interleukin-4 (IL-4) in estrogen receptor-positive human breast cancer cells. J. Biol. Chem. 273:9994-10003.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9994-10003
    • Jackson, J.G.1    White, M.F.2    Yee, D.3
  • 25
    • 0028825748 scopus 로고
    • Tumor necrosis factor alpha-induced phosphorylation of insulin receptor substrate-1 (IRS-1). Possible mechanism for suppression of insulin-stimulated tyrosine phosphorylation of IRS-1
    • Kanety, H., R. Feinstein, M. Z. Papa, R. Hemi, and A. Karasik. 1995. Tumor necrosis factor alpha-induced phosphorylation of insulin receptor substrate-1 (IRS-1). Possible mechanism for suppression of insulin-stimulated tyrosine phosphorylation of IRS-1. J. Biol. Chem. 270:23780-23784.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23780-23784
    • Kanety, H.1    Feinstein, R.2    Papa, M.Z.3    Hemi, R.4    Karasik, A.5
  • 26
    • 0000413462 scopus 로고    scopus 로고
    • Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
    • Kim, T. K., and T. Maniatis. 1996. Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273:1717-1719.
    • (1996) Science , vol.273 , pp. 1717-1719
    • Kim, T.K.1    Maniatis, T.2
  • 27
    • 0031594188 scopus 로고    scopus 로고
    • 14-3-3β protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3′-kinase activity in 3T3L1 adipocytes
    • Kosaki, A., K. Yamada, J. Suga, A. Otaka, and H. Kuzuya. 1998. 14-3-3β protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3′-kinase activity in 3T3L1 adipocytes. J. Biol. Chem. 273:940-944.
    • (1998) J. Biol. Chem. , vol.273 , pp. 940-944
    • Kosaki, A.1    Yamada, K.2    Suga, J.3    Otaka, A.4    Kuzuya, H.5
  • 28
    • 0031594638 scopus 로고    scopus 로고
    • 1-S transition: The SCF connection
    • 1-S transition: the SCF connection. Curr. Opin. Genet. Dev. 8:36-42.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 36-42
    • Krek, W.1
  • 29
    • 0028018858 scopus 로고
    • The phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-1. Stimulation by insulin and inhibition by wortmannin
    • Lam, K., C. L. Carpenter, N. B. Ruderman, J. C. Friel, and K. L. Kelly. 1994. the phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-1. Stimulation by insulin and inhibition by wortmannin. J. Biol. Chem. 269:20648-20652.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20648-20652
    • Lam, K.1    Carpenter, C.L.2    Ruderman, N.B.3    Friel, J.C.4    Kelly, K.L.5
  • 30
    • 0030848782 scopus 로고    scopus 로고
    • A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family
    • Lavan, B. E., V. R. Fantin, E. T. Chang, W. S. Lane, S. R. Keller, and G. E. Lienhard. 1997. A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family. J. Biol. Chem. 272:21403-21407.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21403-21407
    • Lavan, B.E.1    Fantin, V.R.2    Chang, E.T.3    Lane, W.S.4    Keller, S.R.5    Lienhard, G.E.6
  • 31
    • 0030995946 scopus 로고    scopus 로고
    • The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family
    • Lavan, B. E., W. S. Lane, and G. E. Lienhard. 1997. The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family. J. Biol. Chem. 272:11439-11443.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11439-11443
    • Lavan, B.E.1    Lane, W.S.2    Lienhard, G.E.3
  • 32
    • 0033305004 scopus 로고    scopus 로고
    • Enhancement of insulin-like growth factor signaling in human breast cancer: Estrogen regulation of insulin receptor substrate-1 expression in vitro and in vivo
    • Lee, A. V., J. G. Jackson, J. L. Gooch, S. G. Hilsenbeck, E. Coronado-Heinsohn, C. K. Osborne, and D. Yee. 1999. Enhancement of insulin-like growth factor signaling in human breast cancer: estrogen regulation of insulin receptor substrate-1 expression in vitro and in vivo. Mol. Endocrinol. 13:787-796.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 787-796
    • Lee, A.V.1    Jackson, J.G.2    Gooch, J.L.3    Hilsenbeck, S.G.4    Coronado-Heinsohn, E.5    Osborne, C.K.6    Yee, D.7
  • 33
    • 0027496895 scopus 로고
    • Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)
    • Liu, J. P., J. Baker, A. S. Perkins, E. J. Robertson, and A. Efstratiadis. 1993. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 75:59-72.
    • (1993) Cell , vol.75 , pp. 59-72
    • Liu, J.P.1    Baker, J.2    Perkins, A.S.3    Robertson, E.J.4    Efstratiadis, A.5
  • 34
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 35
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti, A. M., M. Treier, and D. Bohmann. 1997. Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275:400-402.
    • (1997) Science , vol.275 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 36
    • 0028036698 scopus 로고
    • Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1, and interleukin-4 stimulation
    • Myers, M. G., Jr., T. C. Grammer, L. M. Wang, X. J. Sun, J. H. Pierce, J. Blenis, and M. F. White. 1994. Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1, and interleukin-4 stimulation. J. Biol. Chem. 269:28783-28789.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28783-28789
    • Myers M.G., Jr.1    Grammer, T.C.2    Wang, L.M.3    Sun, X.J.4    Pierce, J.H.5    Blenis, J.6    White, M.F.7
  • 37
    • 0032128002 scopus 로고    scopus 로고
    • Antigen receptor signaling induces MAP kinase-mediated phosphorylation and degradation of the BCL-6 transcription factor
    • Niu, H., B. H. Ye, and R. Dalla-Favera. 1998. Antigen receptor signaling induces MAP kinase-mediated phosphorylation and degradation of the BCL-6 transcription factor. Genes Dev. 12:1953-1961.
    • (1998) Genes Dev. , vol.12 , pp. 1953-1961
    • Niu, H.1    Ye, B.H.2    Dalla-Favera, R.3
  • 38
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation
    • Noguchi, T., T. Matozaki, K. Horita, Y. Fujioka, and M. Kasuga. 1994. Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation. Mol. Cell. Biol. 14:6674-6682.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 40
    • 0023239937 scopus 로고
    • Biological differences among MCF-7 human breast cancer cell lines from different laboratories
    • Osborne, C. K., K. Hobbs, and J. M. Trent. 1987. Biological differences among MCF-7 human breast cancer cell lines from different laboratories. Breast Cancer Res. Treat. 9:111-121.
    • (1987) Breast Cancer Res. Treat. , vol.9 , pp. 111-121
    • Osborne, C.K.1    Hobbs, K.2    Trent, J.M.3
  • 41
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and J. P. Scott. 1997. Signaling through scaffold, anchoring, and adaptor proteins. Science 278:2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.P.2
  • 42
    • 85039200112 scopus 로고    scopus 로고
    • The p-tyr binding (PTB) domain of insulin receptor substrate (IRS) proteins serves as a substrate for protein kinase B (PKB). Possible involvement of PKB in insulin resistance induced by hyperinsulinemia
    • Paz, K., R. Hemi, D. LeRoith, H. Kanety, and Y. Zick. 1998. The p-tyr binding (PTB) domain of insulin receptor substrate (IRS) proteins serves as a substrate for protein kinase B (PKB). Possible involvement of PKB in insulin resistance induced by hyperinsulinemia. Proc. Endocr. Soc. OR17-2: 75.
    • (1998) Proc. Endocr. Soc. , vol.OR17-2 , pp. 75
    • Paz, K.1    Hemi, R.2    LeRoith, D.3    Kanety, H.4    Zick, Y.5
  • 43
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart, C. M. 1997. Targeting of substrates to the 26S proteasome. FASEB J. 11:1055-1066.
    • (1997) FASEB J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 44
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 45
    • 0033599342 scopus 로고    scopus 로고
    • IGF-I regulates IRS-1 expression in 3T3-L1 adipocytes
    • Rice, K. M., and C. W. Garner. 1999. IGF-I regulates IRS-1 expression in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 255:614-617.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 614-617
    • Rice, K.M.1    Garner, C.W.2
  • 46
    • 0026744181 scopus 로고
    • Regulation of the expression of pp160, a putative insulin receptor signal protein, by insulin, dexamethasone, and 1-methyl-3-isobutylxanthine in 3T3-L1 adipocytes
    • Rice, K. M., G. E. Lienhard, and C. W. Garner. 1992. Regulation of the expression of pp160, a putative insulin receptor signal protein, by insulin, dexamethasone, and 1-methyl-3-isobutylxanthine in 3T3-L1 adipocytes. J. Biol. Chem. 267:10163-10167.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10163-10167
    • Rice, K.M.1    Lienhard, G.E.2    Garner, C.W.3
  • 47
    • 0027280156 scopus 로고
    • Insulin stimulates the degradation of IRS-1 in 3T3-L1 adipocytes
    • Rice, K. M., M. A. Turnbow, and C. W. Garner. 1993. Insulin stimulates the degradation of IRS-1 in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 190:961-967.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 961-967
    • Rice, K.M.1    Turnbow, M.A.2    Garner, C.W.3
  • 48
    • 0032912182 scopus 로고    scopus 로고
    • Insulin receptor substrate 1 is a target for the pure antiestrogen ICI 182,780 in breast cancer cells
    • Salerno, M., D. Sisci, L. Mauro, M. A. Guvakova, S. Ando, and E. Surmacz. 1999. Insulin receptor substrate 1 is a target for the pure antiestrogen ICI 182,780 in breast cancer cells. Int. J. Cancer 81:299-304.
    • (1999) Int. J. Cancer , vol.81 , pp. 299-304
    • Salerno, M.1    Sisci, D.2    Mauro, L.3    Guvakova, M.A.4    Ando, S.5    Surmacz, E.6
  • 49
    • 0031756168 scopus 로고    scopus 로고
    • Insulin receptor substrate-1 and phosphatidylinositol 3-kinase regulate extracellular signal-regulated kinase-dependent and -independent signaling pathways during myogenic differentiation
    • Sarbassov, D. D., and C. A. Peterson. 1998. Insulin receptor substrate-1 and phosphatidylinositol 3-kinase regulate extracellular signal-regulated kinase-dependent and -independent signaling pathways during myogenic differentiation. Mol. Endocrinol. 12:1870-1878.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1870-1878
    • Sarbassov, D.D.1    Peterson, C.A.2
  • 50
    • 0030730246 scopus 로고    scopus 로고
    • Cloning, tissue expression, and chromosomal localization of the mouse IRS-3 gene
    • Sciacchitano, S., and S. I. Taylor. 1997. Cloning, tissue expression, and chromosomal localization of the mouse IRS-3 gene. Endocrinology 138: 4931-4940.
    • (1997) Endocrinology , vol.138 , pp. 4931-4940
    • Sciacchitano, S.1    Taylor, S.I.2
  • 52
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., K. L. Craig, M. Tyers, S. J. Elledge, and J. W. Harper. 1997. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91:209-219.
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 53
    • 0027421453 scopus 로고
    • The insulin receptor substrate (IRS-1) is a PEST protein that is susceptible to calpain degradation in vitro
    • Smith, L. K., M. Bradshaw, D. E. Croall, and C. W. Garner. 1993. The insulin receptor substrate (IRS-1) is a PEST protein that is susceptible to calpain degradation in vitro. Biochem. Biophys. Res. Commun. 196:767-772.
    • (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
  • 54
    • 0030606870 scopus 로고    scopus 로고
    • The insulin-induced down-regulation of IRS-1 in 3T3-L1 adipocytes is mediated by a calcium-dependent thiol protease
    • Smith, L. K., K. M. Rice, and C. W. Garner. 1996. The insulin-induced down-regulation of IRS-1 in 3T3-L1 adipocytes is mediated by a calcium-dependent thiol protease. Mol. Cell. Endocrinol. 122:81-92.
    • (1996) Mol. Cell. Endocrinol. , vol.122 , pp. 81-92
    • Smith, L.K.1    Rice, K.M.2    Garner, C.W.3
  • 56
    • 0000085132 scopus 로고    scopus 로고
    • Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway
    • Sun, X. J., J. L. Goldberg, L. Y. Qiao, and J. J. Mitchell. 1999. Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway. Diabetes 48:1359-1364.
    • (1999) Diabetes , vol.48 , pp. 1359-1364
    • Sun, X.J.1    Goldberg, J.L.2    Qiao, L.Y.3    Mitchell, J.J.4
  • 60
    • 0027967958 scopus 로고
    • Insulin receptor substrate 1 is phosphorylated by the serine kinase activity of phosphatidylinositol 3-kinase
    • Tanti, J. F., T. Gremeaux, E. Van Obberghen, and Y. Le Marchand-Brustel. 1994. Insulin receptor substrate 1 is phosphorylated by the serine kinase activity of phosphatidylinositol 3-kinase. Biochem. J. 304:17-21.
    • (1994) Biochem. J. , vol.304 , pp. 17-21
    • Tanti, J.F.1    Gremeaux, T.2    Van Obberghen, E.3    Le Marchand-Brustel, Y.4
  • 61
    • 0030060965 scopus 로고    scopus 로고
    • Interaction of the molecular weight 85K regulatory subunit of the phosphatidylinositol 3-kinase with the insulin receptor and the insulin-like growth factor-1 (IGF-I) receptor: Comparative study using the yeast two-hybrid system
    • Tartare-Deckert, S., J. Murdaca, D. Sawka-Verhelle, K. H. Holt, J. E. Pessin, and E. Van Obberghen. 1996. Interaction of the molecular weight 85K regulatory subunit of the phosphatidylinositol 3-kinase with the insulin receptor and the insulin-like growth factor-1 (IGF-I) receptor: comparative study using the yeast two-hybrid system. Endocrinology 137:1019-1024.
    • (1996) Endocrinology , vol.137 , pp. 1019-1024
    • Tartare-Deckert, S.1    Murdaca, J.2    Sawka-Verhelle, D.3    Holt, K.H.4    Pessin, J.E.5    Van Obberghen, E.6
  • 62
    • 0032521642 scopus 로고    scopus 로고
    • The mitogen-activated protein (MAP) kinase cascade can either stimulate or inhibit DNA synthesis in primary cultures of rat hepatocytes depending upon whether its activation is acute/phasic or chronic
    • Tombes, R. M., K. L. Auer, R. Mikkelsen, K. Valerie, M. P. Wymann, C. J. Marshall, M. McMahon, and P. Dent. 1998. The mitogen-activated protein (MAP) kinase cascade can either stimulate or inhibit DNA synthesis in primary cultures of rat hepatocytes depending upon whether its activation is acute/phasic or chronic. Biochem. J. 330:1451-1460.
    • (1998) Biochem. J. , vol.330 , pp. 1451-1460
    • Tombes, R.M.1    Auer, K.L.2    Mikkelsen, R.3    Valerie, K.4    Wymann, M.P.5    Marshall, C.J.6    McMahon, M.7    Dent, P.8
  • 63
    • 0028024916 scopus 로고
    • Dexamethasone down-regulation of insulin receptor subsirate-1 in 3T3-L1 adipocytes
    • Turnbow, M. A., S. R. Keller, K. M. Rice, and C. W. Garner. 1994. Dexamethasone down-regulation of insulin receptor subsirate-1 in 3T3-L1 adipocytes. J. Biol. Chem. 269:2516-2520.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2516-2520
    • Turnbow, M.A.1    Keller, S.R.2    Rice, K.M.3    Garner, C.W.4
  • 64
    • 0028641601 scopus 로고
    • Association of insulin receptor substrate-1 with integrins
    • Vuori, K., and E. Ruoslahti. 1994. Association of insulin receptor substrate-1 with integrins. Science 266:1576-1578.
    • (1994) Science , vol.266 , pp. 1576-1578
    • Vuori, K.1    Ruoslahti, E.2
  • 65
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E
    • Won, K. A., and S. I. Reed. 1996. Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15:4182-4193.
    • (1996) EMBO J. , vol.15 , pp. 4182-4193
    • Won, K.A.1    Reed, S.I.2
  • 66
    • 0031171216 scopus 로고    scopus 로고
    • The IRS-signalling system during insulin and cytokine action
    • Yenush, L., and M. F. White. 1997. The IRS-signalling system during insulin and cytokine action. Bioessays 19:491-500.
    • (1997) Bioessays , vol.19 , pp. 491-500
    • Yenush, L.1    White, M.F.2


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