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Volumn 137, Issue 6, 1996, Pages 2362-2366

Reduced phosphorylation of mitogen-activated protein kinase kinase in response to insulin in cells with truncated C-terminal domain of insulin receptor

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; INSULIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; RAF PROTEIN;

EID: 0030011052     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.6.8641187     Document Type: Article
Times cited : (4)

References (46)
  • 1
    • 0023736417 scopus 로고
    • The insulin receptor and the molecular mechanism of insulin action
    • Kahn CR, White MF 1988 The insulin receptor and the molecular mechanism of insulin action. J Clin Invest 82:1151-1156
    • (1988) J Clin Invest , vol.82 , pp. 1151-1156
    • Kahn, C.R.1    White, M.F.2
  • 2
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White MF, Kahn CR 1994 The insulin signaling system. J Biol Chem 269:1-4
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 3
    • 0020065416 scopus 로고
    • Insulin stimulates the phosphorylation of the 95,000 dalton subunit of its own receptor
    • Kasuga M, Karlsson F, Kahn CR 1982 Insulin stimulates the phosphorylation of the 95,000 dalton subunit of its own receptor. Science 215:185-189
    • (1982) Science , vol.215 , pp. 185-189
    • Kasuga, M.1    Karlsson, F.2    Kahn, C.R.3
  • 4
    • 0026748806 scopus 로고
    • The role of insulin receptor kinase domain autophosphorylation in receptor-mediated activities. Analysis with insulin and anti-receptor antibodies
    • 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. Analysis with insulin and anti-receptor antibodies. J Biol Chem 267:13719-13727
    • (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
  • 5
    • 0023240345 scopus 로고
    • Human insulin receptor mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin
    • Chou CK, Dull TJ, Russell ES, Gherzi R, Lebwohl D, Ullrich A, Rosen OM 1987 Human insulin receptor mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin. J Biol Chem 262:1842-1847
    • (1987) J Biol Chem , vol.262 , pp. 1842-1847
    • Chou, C.K.1    Dull, T.J.2    Russell, E.S.3    Gherzi, R.4    Lebwohl, D.5    Ullrich, A.6    Rosen, O.M.7
  • 6
    • 0038856677 scopus 로고
    • Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- And antibody-stimulated glucose uptake and receptor kinase activity
    • Ebina Y, Araki E, Taira M, Shimada F, Mori M, Craik CS, Siddle K, Pierce SB, Roth RA, Rutter WJ 1987 Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity. Proc Natl Acad Sci USA 84:704-708
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 704-708
    • Ebina, Y.1    Araki, E.2    Taira, M.3    Shimada, F.4    Mori, M.5    Craik, C.S.6    Siddle, K.7    Pierce, S.B.8    Roth, R.A.9    Rutter, W.J.10
  • 7
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine kinase residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis L, Clauser E, Morgan DO, Edery M, Roth RA, Rutter WJ 1986 Replacement of insulin receptor tyrosine kinase residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45:721-732
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.A.5    Rutter, W.J.6
  • 8
    • 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 267:16660-16668
    • (1992) J Biol Chem , vol.267 , pp. 16660-16668
    • Wilden, P.A.1    Kahn, C.R.2    Siddle, K.3    White, M.F.4
  • 11
    • 0024358334 scopus 로고
    • Augmented mitogenesis and impaired metabolic signaling mediated by a truncated insulin receptor
    • Thies RS, Ullrich A, McClain DA 1989 Augmented mitogenesis and impaired metabolic signaling mediated by a truncated insulin receptor. J Biol Chem 264:12820-12825
    • (1989) J Biol Chem , vol.264 , pp. 12820-12825
    • Thies, R.S.1    Ullrich, A.2    McClain, D.A.3
  • 12
    • 0023905461 scopus 로고
    • Properties of a human insulin receptor with a COOH-terminal truncation. I. Normal insulin binding, autophosphorylation and endocytosis
    • McClain DA, Maegawa H, Levy J, Huecksteadt T, Dull TJ, Lee J, Ullrich A, Olefsky JM 1988 Properties of a human insulin receptor with a COOH-terminal truncation. I. Normal insulin binding, autophosphorylation and endocytosis. J Biol Chem 263:8904-8911
    • (1988) J Biol Chem , vol.263 , pp. 8904-8911
    • McClain, D.A.1    Maegawa, H.2    Levy, J.3    Huecksteadt, T.4    Dull, T.J.5    Lee, J.6    Ullrich, A.7    Olefsky, J.M.8
  • 13
    • 0023907193 scopus 로고
    • Properties of a human insulin receptor with a C-terminal truncation. II. Truncated receptors have normal kinase activity but are defective in signaling of metabolic effects of insulin
    • Maegawa H, McClain DA, Freidenberg G, Olefsky JM, Napier M, Lipari T, Dull TJ, Lee J, Ullrich A 1988 Properties of a human insulin receptor with a C-terminal truncation. II. Truncated receptors have normal kinase activity but are defective in signaling of metabolic effects of insulin. J Biol Chem 263:8912-8917
    • (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    Lipari, T.6    Dull, T.J.7    Lee, J.8    Ullrich, A.9
  • 14
    • 0027419830 scopus 로고
    • Mechanism of impaired metabolic signaling by a truncated human insulin receptor
    • Begum N, Olefsky JM, Draznin B 1993 Mechanism of impaired metabolic signaling by a truncated human insulin receptor. J Biol Chem 268:7917-7922
    • (1993) J Biol Chem , vol.268 , pp. 7917-7922
    • Begum, N.1    Olefsky, J.M.2    Draznin, B.3
  • 15
    • 0027257212 scopus 로고
    • Insulin activates p21Ras and guanine nucleotide releasing factor in cells expressing wild type and mutant insulin receptors
    • Draznin B, Chang L, Leitner JW, Takata Y, Olefsky JM 1993 Insulin activates p21Ras and guanine nucleotide releasing factor in cells expressing wild type and mutant insulin receptors. J Biol Chem 268:19998-20001
    • (1993) J Biol Chem , vol.268 , pp. 19998-20001
    • Draznin, B.1    Chang, L.2    Leitner, J.W.3    Takata, Y.4    Olefsky, J.M.5
  • 16
    • 0026641090 scopus 로고
    • Activation of mitogen-activated protein kinase kinase by v-raf in NIH 3T3 cells and in vitro
    • Dent P, Haser W, Haystead TAJ, Vincent LA, Roberts TM, Sturgill TW 1992 Activation of mitogen-activated protein kinase kinase by v-raf in NIH 3T3 cells and in vitro. Science 257:1404-1407
    • (1992) Science , vol.257 , pp. 1404-1407
    • Dent, P.1    Haser, W.2    Haystead, T.A.J.3    Vincent, L.A.4    Roberts, T.M.5    Sturgill, T.W.6
  • 21
    • 0028670788 scopus 로고
    • Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
    • Yan M, Dai T, Deak JC, Kyriakis JM, Zon LI, Woodgett JR, Templeton DJ 1994 Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. Nature 372:798-800
    • (1994) Nature , vol.372 , pp. 798-800
    • Yan, M.1    Dai, T.2    Deak, J.C.3    Kyriakis, J.M.4    Zon, L.I.5    Woodgett, J.R.6    Templeton, D.J.7
  • 22
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek AB, Hollenberg SM, Cooper JA 1993 Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 23
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne PH, Viciana PR, Downward J 1993 Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 364:352-355
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 25
    • 0027935756 scopus 로고
    • Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation
    • Hallberg B, Rayter SI, Downward J 1994 Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation. J Biol Chem 269:3913-3916
    • (1994) J Biol Chem , vol.269 , pp. 3913-3916
    • Hallberg, B.1    Rayter, S.I.2    Downward, J.3
  • 26
    • 0001010670 scopus 로고
    • Signal transduction from membrane to cytoplasm: Growth factors and membrane bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity
    • Morrison DH, Kaplan DR, Rapp U, Roberts TM 1988 Signal transduction from membrane to cytoplasm: growth factors and membrane bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity. Proc Natl Acad Sci USA 85:8855-8859
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8855-8859
    • Morrison, D.H.1    Kaplan, D.R.2    Rapp, U.3    Roberts, T.M.4
  • 27
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers SJ, Paterson HF, Marshall CJ 1994 Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369:411-414
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 31
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Rat 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 Rat and effects on its activation. Science 265:1713-1716
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 32
    • 0029071689 scopus 로고
    • 14-3-3 is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3 and Ras-independent manner
    • Michaud NR, Fabian JR, Mathes KD, Morrison DK 1995 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3 and Ras-independent manner. Mol Cell Biol 15:3390-3397
    • (1995) Mol Cell Biol , vol.15 , pp. 3390-3397
    • Michaud, N.R.1    Fabian, J.R.2    Mathes, K.D.3    Morrison, D.K.4
  • 34
    • 0027337519 scopus 로고
    • Complexes of Ras-GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie SA, Willumsen BM, Weber MJ, Wolfman A 1993 Complexes of Ras-GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 260:1658-1661
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 35
    • 0029042701 scopus 로고
    • Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro
    • Dent P, Reardon DB, Morrison DK, Sturgill TW 1995 Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro. Mol Cell Biol 15:4125-4135
    • (1995) Mol Cell Biol , vol.15 , pp. 4125-4135
    • Dent, P.1    Reardon, D.B.2    Morrison, D.K.3    Sturgill, T.W.4
  • 36
    • 0028924793 scopus 로고
    • Ras-dependent and -independent pathways target the mitogen-activated protein kinase network in macrophages
    • Büscher D, Hipskind RA, Krautwald S, Reimann T, Baccarini M 1995 Ras-dependent and -independent pathways target the mitogen-activated protein kinase network in macrophages. Mol Cell Biol 15:466-475
    • (1995) Mol Cell Biol , vol.15 , pp. 466-475
    • Büscher, D.1    Hipskind, R.A.2    Krautwald, S.3    Reimann, T.4    Baccarini, M.5
  • 38
    • 0026690922 scopus 로고
    • Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells
    • Seger R, Ahn NG, Posada J, Munar ES, Jensen AM, Cooper JA, Cobb MH, Krebs EG 1992 Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J Biol Chem 267:14373-14381
    • (1992) J Biol Chem , vol.267 , pp. 14373-14381
    • Seger, R.1    Ahn, N.G.2    Posada, J.3    Munar, E.S.4    Jensen, A.M.5    Cooper, J.A.6    Cobb, M.H.7    Krebs, E.G.8
  • 39
    • 0027424367 scopus 로고
    • Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases
    • Zheng C-F, Guan K-L 1993 Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases. J Biol Chem 268:23933-23939
    • (1993) J Biol Chem , vol.268 , pp. 23933-23939
    • Zheng, C.-F.1    Guan, K.-L.2
  • 40
    • 0028074621 scopus 로고
    • Ras-dependent growth factor regulation of MEK kinase in PC12 cells
    • Lange-Carter CA, Johnson GL 1994 Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science 265:1458-1461
    • (1994) Science , vol.265 , pp. 1458-1461
    • Lange-Carter, C.A.1    Johnson, G.L.2
  • 41
    • 0029077563 scopus 로고
    • Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1)
    • Russell M, Lange-Carter CA, Johnson GL 1995 Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1). J Biol Chem 270:11757-11760
    • (1995) J Biol Chem , vol.270 , pp. 11757-11760
    • Russell, M.1    Lange-Carter, C.A.2    Johnson, G.L.3
  • 43
    • 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 269:10127-10132
    • (1994) J Biol Chem , vol.269 , pp. 10127-10132
    • Fingar, D.C.1    Birnbaum, M.J.2
  • 44
    • 0028297696 scopus 로고
    • Activation of the Ras/mitogen-activated protein kinase signaling pathway alone is not sufficient to induce glucose uptake in 3T3-L1 adipocytes
    • van den Berghe N, Ouwens DM, Maassen JA, van Mackelenbergh MGH, Sips HCM, Krans MJ 1994 Activation of the Ras/mitogen-activated protein kinase signaling pathway alone is not sufficient to induce glucose uptake in 3T3-L1 adipocytes. Mol Cell Biol 14:2372-2377
    • (1994) Mol Cell Biol , vol.14 , pp. 2372-2377
    • Van Den Berghe, N.1    Ouwens, D.M.2    Maassen, J.A.3    Van Mackelenbergh, M.G.H.4    Sips, H.C.M.5    Krans, M.J.6
  • 45
    • 0028308412 scopus 로고
    • Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation
    • Cheatham B, Vlahos CJ, Cheatham L, Wang L, Blenis J, Kahn CR 1994 Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation. Mol Cell Biol 14:4902-4911
    • (1994) Mol Cell Biol , vol.14 , pp. 4902-4911
    • Cheatham, B.1    Vlahos, C.J.2    Cheatham, L.3    Wang, L.4    Blenis, J.5    Kahn, C.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.