메뉴 건너뛰기




Volumn 139, Issue 12, 1998, Pages 4984-4990

Effects of general receptor for phosphoinositides 1 on insulin and insulin-like growth factor I-induced cytoskeletal rearrangement, glucose transporter-4 translocation, and deoxyribonucleic acid synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DNA; GLUCOSE TRANSPORTER; GUANINE NUCLEOTIDE BINDING PROTEIN; INSULIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITIDE RECEPTOR; PHOSPHATIDYLINOSITOL KINASE; RECEPTOR PROTEIN; SOMATOMEDIN C; UNCLASSIFIED DRUG;

EID: 0031785519     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.139.12.6351     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0024601010 scopus 로고
    • PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells
    • Auger KR, Serunian LA, Soltoff SP, Libby P, Cantley LC 1989 PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. Cell 57:167-175
    • (1989) Cell , vol.57 , pp. 167-175
    • Auger, K.R.1    Serunian, L.A.2    Soltoff, S.P.3    Libby, P.4    Cantley, L.C.5
  • 3
    • 0029823946 scopus 로고    scopus 로고
    • A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphophate formation in chemoattractant-stimulated human neutrophils
    • Ptasznik A, Prossnitz ER, Yoshikawa D, Smrcka A, Bokoch GM 1996 A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphophate formation in chemoattractant-stimulated human neutrophils. J Biol Chem 271:25204-25207
    • (1996) J Biol Chem , vol.271 , pp. 25204-25207
    • Ptasznik, A.1    Prossnitz, E.R.2    Yoshikawa, D.3    Smrcka, A.4    Bokoch, G.M.5
  • 4
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by Gβ-γ subunits
    • Stephans L, Smrcka A, Cooke FT, Jackson TJ, Sternweis P, Hawkins PT 1994 A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by Gβ-γ subunits. Cell 77:83-93
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephans, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.J.4    Sternweis, P.5    Hawkins, P.T.6
  • 5
    • 0027366440 scopus 로고
    • Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphophate-a new signaling pathway
    • Stephans LR, Jackson Tr, Hawkins PT 1993 Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphophate-a new signaling pathway. Biochim Biophys Acta 1179:27-75
    • (1993) Biochim Biophys Acta , vol.1179 , pp. 27-75
    • Stephans, L.R.1    Jackson, Tr.2    Hawkins, P.T.3
  • 6
    • 0028143039 scopus 로고
    • Microinjection of the SH2 domain of the 85-kilodalton subunit of phosphatidylinositol 3-kinase inhibits insulin-induced DNA synthesis and c-fos expression
    • Jhun BH, Rose DW, Seely BL, Rameh L, Cantley L, Saltiel AR, Olefsky JM 1994 Microinjection of the SH2 domain of the 85-kilodalton subunit of phosphatidylinositol 3-kinase inhibits insulin-induced DNA synthesis and c-fos expression. Mol Cell Biol 14:7466-7475
    • (1994) Mol Cell Biol , vol.14 , pp. 7466-7475
    • Jhun, B.H.1    Rose, D.W.2    Seely, B.L.3    Rameh, L.4    Cantley, L.5    Saltiel, A.R.6    Olefsky, J.M.7
  • 7
    • 0029973135 scopus 로고    scopus 로고
    • Activated phosphatylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocarion in 3T3-L1 adipocytes
    • Martin SS, Haruta T, Morris A, Klippel A, Williams LT, Olefsky JM 1996 Activated phosphatylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocarion 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.3    Klippel, A.4    Williams, L.T.5    Olefsky, J.M.6
  • 8
    • 0030575539 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase and the regulation of cell growth
    • Carpenter CL, Cantley LC 1996 Phosphoinositide 3-kinase and the regulation of cell growth. Biochim Biophys Acta 1288:M11-M16
    • (1996) Biochim Biophys Acta , vol.1288
    • Carpenter, C.L.1    Cantley, L.C.2
  • 9
    • 0029813084 scopus 로고    scopus 로고
    • Role of PI 3-kinase and SH-PTP2 in insulin action
    • Kasuga M 1996 Role of PI 3-kinase and SH-PTP2 in insulin action. Diabetic Med 13:S87-S89
    • (1996) Diabetic Med , vol.13
    • Kasuga, M.1
  • 10
    • 0030470754 scopus 로고
    • The role of phosphoinositide 3-kinase in insulin signaling
    • Shepherd PR, Nave BT, O'Rahilly S 1946 The role of phosphoinositide 3-kinase in insulin signaling. J Mol Endocrinol 17:175-184
    • (1946) J Mol Endocrinol , vol.17 , pp. 175-184
    • Shepherd, P.R.1    Nave, B.T.2    O'Rahilly, S.3
  • 12
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker A, Cantley LC 1997 Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387:673676-676
    • (1997) Nature , vol.387 , pp. 673676-673676
    • Toker, A.1    Cantley, L.C.2
  • 13
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol 3-OH kinase signal transduction
    • Burgering BM, Coffer PJ 1995 Protein kinase B (c-Akt) in phosphatidylinositol 3-OH kinase signal transduction. Nature 376:599-602
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 14
    • 0029810181 scopus 로고    scopus 로고
    • Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation
    • Kohn AD, Takeuchi F, Roth A 1996 Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J Biol Chem 271:21920-21926
    • (1996) J Biol Chem , vol.271 , pp. 21920-21926
    • Kohn, A.D.1    Takeuchi, F.2    Roth, A.3
  • 15
    • 0002956168 scopus 로고
    • The protein kinase encoded the akt proto-ocogene is a target of the PDGF-activated phosphoinositol 3-kinase
    • Franke TF 1495 The protein kinase encoded the akt proto-ocogene is a target of the PDGF-activated phosphoinositol 3-kinase. Cell 81:1-20
    • (1495) Cell , vol.81 , pp. 1-20
    • Franke, T.F.1
  • 16
    • 0027193913 scopus 로고
    • Insulin-induced circular membrane ruffling on rat 1 cells expressing a high number of human insulin receptors: Circular ruffles caused by rapid actin reorganization exhibit high density of insulin receptors and phosphotyrosines
    • Li SL, Miyata Y, Yahara I, Fujita-Yamaguchi Y 1993 Insulin-induced circular membrane ruffling on rat 1 cells expressing a high number of human insulin receptors: circular ruffles caused by rapid actin reorganization exhibit high density of insulin receptors and phosphotyrosines. Exp Cell Res 205:353-360
    • (1993) Exp Cell Res , vol.205 , pp. 353-360
    • Li, S.L.1    Miyata, Y.2    Yahara, I.3    Fujita-Yamaguchi, Y.4
  • 17
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley JA, Paterson FH, Johnston CL, Diekmann D, Hall A 1992 The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell 70:401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, J.A.1    Paterson, F.H.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 19
    • 0029850645 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is necessary and sufficient for insulin-stimulated stress fiber breakdown
    • Martin SS, Rose DW, Saltiel AR, Klippel A, Williams LT, Olefsky JM 1996 Phosphatidylinositol 3-kinase is necessary and sufficient for insulin-stimulated stress fiber breakdown. Endocrinolgy 137:5045-5054
    • (1996) Endocrinolgy , vol.137 , pp. 5045-5054
    • Martin, S.S.1    Rose, D.W.2    Saltiel, A.R.3    Klippel, A.4    Williams, L.T.5    Olefsky, J.M.6
  • 20
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by the posphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund J, Guilherme A, Holik JJ, Virbasius J, V, Chawla A, Czech MP 1997 Signaling by the posphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275:1927-1930
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 22
    • 0025923845 scopus 로고
    • Intracellular targeting of the insulin-regulatable glucose transporter (GLUT4) is isoform specific and independent of cell type
    • Haney PM, Slot JW, Piper RC, James DE, Mueckler M 1991 Intracellular targeting of the insulin-regulatable glucose transporter (GLUT4) is isoform specific and independent of cell type. J Cell Biol 114:689-699
    • (1991) J Cell Biol , vol.114 , pp. 689-699
    • Haney, P.M.1    Slot, J.W.2    Piper, R.C.3    James, D.E.4    Mueckler, M.5
  • 23
    • 0028875678 scopus 로고
    • Insulin-stimulated GLUT 4 translocation is mediated by a divergent intracellular signaling pathway
    • Haruta T, Morris AJ, Rose DW, Nelson JG, Mueckler M, Olefsky JM 1995 Insulin-stimulated GLUT 4 translocation is mediated by a divergent intracellular signaling pathway. J Biol Chem 270:27991-27994
    • (1995) J Biol Chem , vol.270 , pp. 27991-27994
    • Haruta, T.1    Morris, A.J.2    Rose, D.W.3    Nelson, J.G.4    Mueckler, M.5    Olefsky, J.M.6
  • 24
    • 0027391632 scopus 로고
    • Direct analysis of the binding of the abl Src homology domain to the activated epidermal growth factor receptor
    • Zhu G, Decker SJ, Mayer BJ, Saltiel AR 1993 Direct analysis of the binding of the abl Src homology domain to the activated epidermal growth factor receptor. J Biol Chem 268:1775-1779
    • (1993) J Biol Chem , vol.268 , pp. 1775-1779
    • Zhu, G.1    Decker, S.J.2    Mayer, B.J.3    Saltiel, A.R.4
  • 25
    • 0023665224 scopus 로고
    • A mutant insulin receptor with defective tyrosine kinase displays no biologic activity and does undergo endocytosis
    • McClain DA, Maegawa H, Lee J, Dull TJ, Ulrich A, Olefsky JM 1987 A mutant insulin receptor with defective tyrosine kinase displays no biologic activity and does undergo endocytosis. J Biol Chem 262:14663-14671
    • (1987) J Biol Chem , vol.262 , pp. 14663-14671
    • McClain, D.A.1    Maegawa, H.2    Lee, J.3    Dull, T.J.4    Ulrich, A.5    Olefsky, J.M.6
  • 26
    • 0016698833 scopus 로고
    • Interaction of actin with phalloidin: Polymerization and stabilization of F-actin
    • Dancker P, Low I, Hasselbach W, Wieland T 1975 Interaction of actin with phalloidin: polymerization and stabilization of F-actin. Biochim Biophys Acta 400:407-414
    • (1975) Biochim Biophys Acta , vol.400 , pp. 407-414
    • Dancker, P.1    Low, I.2    Hasselbach, W.3    Wieland, T.4
  • 27
    • 0030766987 scopus 로고    scopus 로고
    • A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytosceletal rearrangements
    • D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst I 1997 A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytosceletal rearrangements. EMBO J 16:5445-5454
    • (1997) EMBO J , vol.16 , pp. 5445-5454
    • D'Souza-Schorey, C.1    Boshans, R.L.2    McDonough, M.3    Stahl, P.D.4    Van Aelst, I.5
  • 29
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual AS, Yatsula BA, Bar-Sagi D 1998 Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279:560-563
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 32
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Rac-1-interacting protein involved in membrane ruffling
    • Van Aelst L, Joneson T, Bar-Sagi D 1996 Identification of a novel Rac-1-interacting protein involved in membrane ruffling. EMBO J 15:3778-3786
    • (1996) EMBO J , vol.15 , pp. 3778-3786
    • Van Aelst, L.1    Joneson, T.2    Bar-Sagi, D.3
  • 33
    • 0028925711 scopus 로고
    • Rho-related proteins: Actin cytoskeleton and cell cycle
    • Ridley JA 1995 Rho-related proteins: actin cytoskeleton and cell cycle. Curr Opin Gen Dev 5:30
    • (1995) Curr Opin Gen Dev , vol.5 , pp. 30
    • Ridley, J.A.1
  • 34
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong LD, Traynor-Kaplan A, Bokoch GM, Schwartz MA 1994 The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79:507-513
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 35
    • 0028174102 scopus 로고
    • α-Actinin and vinculin are P1P2-binding proteins involved in signaling by tyrosine kinase
    • Fukami K, Endo T, Imamura M, Takenawa T 1994 α-Actinin and vinculin are P1P2-binding proteins involved in signaling by tyrosine kinase. J Biol Chem 269:1518-1522
    • (1994) J Biol Chem , vol.269 , pp. 1518-1522
    • Fukami, K.1    Endo, T.2    Imamura, M.3    Takenawa, T.4
  • 36
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T 1992 Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function. Nature 359:150-152
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 38
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu Q, Klippel A, Muslin AJ, Fantl WJ, Williams LT 1995 Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 268:100-102
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.