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Volumn 11, Issue 13, 1997, Pages 1911-1923

Interaction of wild type and dominant-negative p55(PIK) regulatory subunit of phosphatidylinositol 3-kinase with insulin-like growth factor-1 signaling proteins

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SUBUNIT; SOMATOMEDIN C; WORTMANNIN;

EID: 0030784680     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.11.13.0029     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman M, Downes CP, Keeler M, Keller T, Cantley L 1988 Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 322:644-646
    • (1988) Nature , vol.322 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 3
    • 0028892253 scopus 로고
    • 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins
    • 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins. Cell 83:821-830
    • (1995) Cell , vol.83 , pp. 821-830
    • Rameh, L.E.1    Chen, C.-S.2    Cantley, L.C.3
  • 4
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao R, Cooper GM 1995 Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science 267:2003-2006
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 7
    • 0029973135 scopus 로고    scopus 로고
    • Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes
    • Martin SS, Haruta T, Morris AJ, Klippel A, Williams LT, Olefsky JM 1996 Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes. J Biol Chem 271:17605-17608
    • (1996) J Biol Chem , vol.271 , pp. 17605-17608
    • Martin, S.S.1    Haruta, T.2    Morris, A.J.3    Klippel, A.4    Williams, L.T.5    Olefsky, J.M.6
  • 8
    • 0030054398 scopus 로고    scopus 로고
    • Overexpression of catalytic subunit p110α of phosphatidylinositol 3-kinase increases glucose transport activity with translocation of glucose transporters in 3T3-L1 adipocytes
    • Katagiri H, Asano T, Ishihara H, Inukai K, Shibasaki Y, Kikuchi M, Yazaki Y, Oka Y 1996 Overexpression of catalytic subunit p110α of phosphatidylinositol 3-kinase increases glucose transport activity with translocation of glucose transporters in 3T3-L1 adipocytes. J Biol Chem 271:16987-16990
    • (1996) J Biol Chem , vol.271 , pp. 16987-16990
    • Katagiri, H.1    Asano, T.2    Ishihara, H.3    Inukai, K.4    Shibasaki, Y.5    Kikuchi, M.6    Yazaki, Y.7    Oka, Y.8
  • 10
    • 0026487847 scopus 로고
    • Interaction of the p85 subunit of PI-3 kinase ans its N-terminal SH2 domain with a PDGF receptor phosphorylation site: Structural features and analysis of conformational changes
    • Panayotou G, Bax B, Gout I, Federwish M, Wroblowski B, Dhand R, Fry MJ, Blundell TL, Wollmer A, Waterfield MD 1992 Interaction of the p85 subunit of PI-3 kinase ans its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J 11:4261-4272
    • (1992) EMBO J , vol.11 , pp. 4261-4272
    • Panayotou, G.1    Bax, B.2    Gout, I.3    Federwish, M.4    Wroblowski, B.5    Dhand, R.6    Fry, M.J.7    Blundell, T.L.8    Wollmer, A.9    Waterfield, M.D.10
  • 11
    • 0027393849 scopus 로고
    • Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation
    • Shoelson SE, Sivaraja M, Williams KP, Hu P, Schlessinger J, Weiss MA 1993 Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation. EMBO J 12:795-802
    • (1993) EMBO J , vol.12 , pp. 795-802
    • Shoelson, S.E.1    Sivaraja, M.2    Williams, K.P.3    Hu, P.4    Schlessinger, J.5    Weiss, M.A.6
  • 13
    • 0029913340 scopus 로고    scopus 로고
    • Insulin receptor substrate 1 binds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain
    • Antonetti DA, Algenstaedt P, Kahn CR 1996 Insulin receptor substrate 1 binds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain. Mol Cell Biol 16:2195-2203
    • (1996) Mol Cell Biol , vol.16 , pp. 2195-2203
    • Antonetti, D.A.1    Algenstaedt, P.2    Kahn, C.R.3
  • 15
    • 0028957113 scopus 로고
    • Molecular and cellular aspects of the insulin-like growth factor I receptor
    • LeRoith D, Werner H, Beitner-Johnson D, Roberts CTJ 1995 Molecular and cellular aspects of the insulin-like growth factor I receptor. Endocr Rev 16:143-163
    • (1995) Endocr Rev , vol.16 , pp. 143-163
    • LeRoith, D.1    Werner, H.2    Beitner-Johnson, D.3    Roberts, C.T.J.4
  • 16
    • 0027512244 scopus 로고
    • The insulin and insulin-like growth factor-1 receptor substrate IRS-1 associates with and activates phosphatidylinositol 3-kinase in vitro
    • Giorgetti S, Ballotti R, Kowalski-Chauvel A, Tartare S, Van Obberghen E 1993 The insulin and insulin-like growth factor-1 receptor substrate IRS-1 associates with and activates phosphatidylinositol 3-kinase in vitro. J Biol Chem 268:7358-7364
    • (1993) J Biol Chem , vol.268 , pp. 7358-7364
    • Giorgetti, S.1    Ballotti, R.2    Kowalski-Chauvel, A.3    Tartare, S.4    Van Obberghen, E.5
  • 17
    • 0028142280 scopus 로고
    • Insulin-like growth factor-I mediated association of p85 phosphatidylinositol 3-kinase with pp185: Requirement of SH2 domains for in vivo interaction
    • Altschuler D, Yamamoto K, Lapetina EG 1994 Insulin-like growth factor-I mediated association of p85 phosphatidylinositol 3-kinase with pp185: requirement of SH2 domains for in vivo interaction. Mol Endocrinol 8:1139-1146
    • (1994) Mol Endocrinol , vol.8 , pp. 1139-1146
    • Altschuler, D.1    Yamamoto, K.2    Lapetina, E.G.3
  • 18
    • 0026753401 scopus 로고
    • Association of phosphorylated insulin-like growth factor-I receptor with the SH2 domains of phosphatidylinositol 3-kinase p85
    • Yamamoto K, Altschuler D, Wood E, Horlick K, Jacobs S, Lapetina EG 1992 Association of phosphorylated insulin-like growth factor-I receptor with the SH2 domains of phosphatidylinositol 3-kinase p85. J Biol Chem 16: 11337-11343
    • (1992) J Biol Chem , vol.16 , pp. 11337-11343
    • Yamamoto, K.1    Altschuler, D.2    Wood, E.3    Horlick, K.4    Jacobs, S.5    Lapetina, E.G.6
  • 19
    • 0029079651 scopus 로고
    • Localization of the insulin-like growth factor I receptor binding sites for the SH2 domain proteins p85, Syp, and GTPase activating protein
    • Seely BL, Reichart DR, Staubs PS, Jhun BH, Hsu D, Maegawa H, Milarski KL, Saltiel AR, Olefsky JM 1995 Localization of the insulin-like growth factor I receptor binding sites for the SH2 domain proteins p85, Syp, and GTPase activating protein. J Biol Chem 270:19151-19157
    • (1995) J Biol Chem , vol.270 , pp. 19151-19157
    • Seely, B.L.1    Reichart, D.R.2    Staubs, P.S.3    Jhun, B.H.4    Hsu, D.5    Maegawa, H.6    Milarski, K.L.7    Saltiel, A.R.8    Olefsky, J.M.9
  • 20
    • 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-1) receptor: Comparative study using the yeast two-hybrid system
    • Tartare-Deckert S, Murdaca J, Sawka-Verhelle D, Holt KH, Pessin JE, Van Obberghen E 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-1) 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
  • 21
    • 0029085477 scopus 로고
    • Interaction of p85 subunit of PI 3-kinase with insulin and IGF-1 receptors analysed by using the two-hybrid system
    • Lamothe B, Bucchini D, Jami J, Joshi RL 1995 Interaction of p85 subunit of PI 3-kinase with insulin and IGF-1 receptors analysed by using the two-hybrid system. FEBS Lett 373:51-55
    • (1995) FEBS Lett , vol.373 , pp. 51-55
    • Lamothe, B.1    Bucchini, D.2    Jami, J.3    Joshi, R.L.4
  • 22
    • 0028133016 scopus 로고
    • The insulin-like growth factor-1 system in the rat cerebellum: Developmental regulation and role in neuronal survival and differentiation
    • Torres-Aleman I, Pons S, Arevalo MA 1994 The insulin-like growth factor-1 system in the rat cerebellum: developmental regulation and role in neuronal survival and differentiation. J Neurosci Res 39:117-126
    • (1994) J Neurosci Res , vol.39 , pp. 117-126
    • Torres-Aleman, I.1    Pons, S.2    Arevalo, M.A.3
  • 23
    • 0028819745 scopus 로고
    • Evidence for a differential interaction of Shc and the insulin receptor substrate 1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system
    • Tartare-Deckert S, Sawka-Verhelle D, Murdaca J, Van Obberghen E 1995 Evidence for a differential interaction of Shc and the insulin receptor substrate 1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system. J Biol Chem 270:23456-23460
    • (1995) J Biol Chem , vol.270 , pp. 23456-23460
    • Tartare-Deckert, S.1    Sawka-Verhelle, D.2    Murdaca, J.3    Van Obberghen, E.4
  • 24
    • 0029866195 scopus 로고    scopus 로고
    • Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786
    • Sawka-Verhelle D, Tartare-Deckert S, White MF, Van Obberghen E 1996 Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786. J Biol Chem 271:5980-5983
    • (1996) J Biol Chem , vol.271 , pp. 5980-5983
    • Sawka-Verhelle, D.1    Tartare-Deckert, S.2    White, M.F.3    Van Obberghen, E.4
  • 25
    • 0029824779 scopus 로고    scopus 로고
    • Interaction of SH2-containing protein tyrosine phosphatase 2 with the insulin receptor and the insulin-like growth factor-I receptor: Studies of the domains involved using the yeast two-hybrid system
    • Rocchi S, Tartare-Deckert S, Sawka-Verhelle D, Gamha A, Van Obberghen E 1996 Interaction of SH2-containing protein tyrosine phosphatase 2 with the insulin receptor and the insulin-like growth factor-I receptor: studies of the domains involved using the yeast two-hybrid system. Endocrinology 137:4944-4952
    • (1996) Endocrinology , vol.137 , pp. 4944-4952
    • Rocchi, S.1    Tartare-Deckert, S.2    Sawka-Verhelle, D.3    Gamha, A.4    Van Obberghen, E.5
  • 26
    • 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
  • 27
    • 0027425064 scopus 로고
    • Structure-function relationship of the insulin-like growth factor-I receptor tyrosine kinase
    • Gronborg M, Wulf BS, Rasmussen JS, Kjeldsen T, Gammeltoft S 1993 Structure-function relationship of the insulin-like growth factor-I receptor tyrosine kinase. J Biol Chem 268:23435-23440
    • (1993) J Biol Chem , vol.268 , pp. 23435-23440
    • Gronborg, M.1    Wulf, B.S.2    Rasmussen, J.S.3    Kjeldsen, T.4    Gammeltoft, S.5
  • 28
    • 0027955344 scopus 로고
    • Essential role of tyrosine residues 1131, 1135, and 1136 of the insulin-like growth factor-I (IGF-1) receptor in IGF-1 action
    • Kato H, Faria TN, Stannard B, Roberts CT, LeRoith D 1994 Essential role of tyrosine residues 1131, 1135, and 1136 of the insulin-like growth factor-I (IGF-1) receptor in IGF-1 action. Mol Endocrinol 8:40-50
    • (1994) Mol Endocrinol , vol.8 , pp. 40-50
    • Kato, H.1    Faria, T.N.2    Stannard, B.3    Roberts, C.T.4    LeRoith, D.5
  • 30
    • 0028120902 scopus 로고
    • Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits
    • Holt KH, Olson AN, Scott Moye-Rowley W, Pessin JE 1994 Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits. Mol Cell Biol 14:42-49
    • (1994) Mol Cell Biol , vol.14 , pp. 42-49
    • Holt, K.H.1    Olson, A.N.2    Scott Moye-Rowley, W.3    Pessin, J.E.4
  • 33
    • 0028142414 scopus 로고
    • Potent activation of phosphatidylinositol 3′-kinase by single phosphotyrosine peptides derived from insulin receptor substrate 1 containing two YMXM motifs for binding SH2 domains
    • Herbst JJ, Andrews G, Contillo L, Lamphere L, Gardner J, Lienhard GE, Gibbs EM 1994 Potent activation of phosphatidylinositol 3′-kinase by single phosphotyrosine peptides derived from insulin receptor substrate 1 containing two YMXM motifs for binding SH2 domains. Biochemistry 33:9376-9381
    • (1994) Biochemistry , vol.33 , pp. 9376-9381
    • Herbst, J.J.1    Andrews, G.2    Contillo, L.3    Lamphere, L.4    Gardner, J.5    Lienhard, G.E.6    Gibbs, E.M.7
  • 34
    • 0029966086 scopus 로고    scopus 로고
    • Insulin-mediated targeting of phosphatidylinositol 3-kinase to GLUT4-containing vesicles
    • Heller-Harrison RA, Morin M, Guilherme A, Czech MP 1996 Insulin-mediated targeting of phosphatidylinositol 3-kinase to GLUT4-containing vesicles. J Biol Chem 271:10200-10204
    • (1996) J Biol Chem , vol.271 , pp. 10200-10204
    • Heller-Harrison, R.A.1    Morin, M.2    Guilherme, A.3    Czech, M.P.4
  • 36
  • 37
    • 0027967958 scopus 로고
    • Insulin receptor substrate 1 is phosphorylated by the serine kinase activity of phosphatidylinositol 3-kinase
    • Tanti J-F, Gremeaux T, Van Obberghen E, Le Marchand-Brustel Y 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
  • 38
    • 0028023002 scopus 로고
    • Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling
    • Tanti J-F, Grémeaux T, Van Obberghen E, Le Marchand-Brustel Y 1994 Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling. J Biol Chem 269:6051-6057
    • (1994) J Biol Chem , vol.269 , pp. 6051-6057
    • Tanti, J.-F.1    Grémeaux, T.2    Van Obberghen, E.3    Le Marchand-Brustel, Y.4
  • 39
    • 15844389443 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action
    • Mothe I, Van Obberghen E 1996 Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action. J Biol Chem 271:11222-11227
    • (1996) J Biol Chem , vol.271 , pp. 11222-11227
    • Mothe, I.1    Van Obberghen, E.2
  • 40
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St. Jean A, Woods RA, Schiestl RH 1992 Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20:1425-1426
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425-1426
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 42
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller JH 1972 Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 633-640
    • (1972) Experiments in Molecular Genetics , pp. 633-640
    • Miller, J.H.1
  • 44
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H 1987 High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7:2745-2752
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2


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