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Volumn 9, Issue 3, 1999, Pages 136-145

Transformation mediated by RhoA requires activity of ROCK kinases

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EID: 0033545354     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80067-0     Document Type: Article
Times cited : (189)

References (32)
  • 1
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L, D'Souza-Schorey C: Rho GTPases and signaling networks. Genes Dev 1997, 11:2295-2322.
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 2
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson MF, Ashworth A, Hall A: An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 1995, 269:1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 3
    • 0032537819 scopus 로고    scopus 로고
    • Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/ Cip1
    • Olson MF, Paterson HF, Marshall CJ: Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/ Cip1. Nature 1998, 394:295-299.
    • (1998) Nature , vol.394 , pp. 295-299
    • Olson, M.F.1    Paterson, H.F.2    Marshall, C.J.3
  • 4
    • 15644378138 scopus 로고    scopus 로고
    • Geranylgeranylated rho small GTPase(s) are essential for the degradation of p27Kip1 and facilitate the progression from G1 to S phase in growth-stimulated rat FRTL-5 cells
    • Hirai A, Nakamura S, Noguchi Y, Yasuda T, Kitagawa M, Tatsuno I, Oeda T, Tahara K, Terano T, Narumiya S, et al.: Geranylgeranylated rho small GTPase(s) are essential for the degradation of p27Kip1 and facilitate the progression from G1 to S phase in growth-stimulated rat FRTL-5 cells. J Biol Chem 1997, 272:13-16.
    • (1997) J Biol Chem , vol.272 , pp. 13-16
    • Hirai, A.1    Nakamura, S.2    Noguchi, Y.3    Yasuda, T.4    Kitagawa, M.5    Tatsuno, I.6    Oeda, T.7    Tahara, K.8    Terano, T.9    Narumiya, S.10
  • 5
    • 0031453368 scopus 로고    scopus 로고
    • Ras-stimulated extracellular signal-related kinase 1 and RhoA activities coordinate platelet-derived growth factor-induced G1 progression through the independent regulation of cyclin D1 and p27
    • Weber JD, Hu W, Jefcoat SC Jr, Raben DM, Baldassare JJ: Ras-stimulated extracellular signal-related kinase 1 and RhoA activities coordinate platelet-derived growth factor-induced G1 progression through the independent regulation of cyclin D1 and p27. J Biol Chem 1997, 272:32966-32971.
    • (1997) J Biol Chem , vol.272 , pp. 32966-32971
    • Weber, J.D.1    Hu, W.2    Jefcoat Jr., S.C.3    Raben, D.M.4    Baldassare, J.J.5
  • 7
    • 0032473351 scopus 로고    scopus 로고
    • RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation
    • Sahai E, Alberts AS, Treisman R: RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J 1998, 17:1350-1361.
    • (1998) EMBO J , vol.17 , pp. 1350-1361
    • Sahai, E.1    Alberts, A.S.2    Treisman, R.3
  • 9
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung T, Chen XQ, Manser E, Lim L: The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol Cell Biol 1996, 16:5313-5327.
    • (1996) Mol Cell Biol , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 10
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki T, Naito M, Fujisawa K, Maekawa M, Watanabe N, Saito Y, Narumiya S: p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett 1997, 404:118-124.
    • (1997) FEBS Lett , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6    Narumiya, S.7
  • 13
    • 0031878095 scopus 로고    scopus 로고
    • Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading
    • Tominaga T, Barber DL: Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading. Mol Biol Cell 1998, 9:2287-2303.
    • (1998) Mol Biol Cell , vol.9 , pp. 2287-2303
    • Tominaga, T.1    Barber, D.L.2
  • 14
    • 0032541338 scopus 로고    scopus 로고
    • p160ROCK mediates RhoA activation of Na-H exchange
    • Tominaga T, Ishizaki T, Narumiya S, Barber DL: p160ROCK mediates RhoA activation of Na-H exchange. EMBO J 1998, 17:4712-4722.
    • (1998) EMBO J , vol.17 , pp. 4712-4722
    • Tominaga, T.1    Ishizaki, T.2    Narumiya, S.3    Barber, D.L.4
  • 19
    • 0030777243 scopus 로고    scopus 로고
    • Integrin signaling: Specificity and control of cell survival and cell cycle progression
    • Giancotti FG: Integrin signaling: specificity and control of cell survival and cell cycle progression. Curr Opin Cell Biol 1997, 9:691-700.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 691-700
    • Giancotti, F.G.1
  • 20
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/ rac GTPases
    • Hotchin NA, Hall A: The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/ rac GTPases. J Cell Biol 1995, 131:1857-1865.
    • (1995) J Cell Biol , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 21
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the rho family of GTPases
    • Clark EA, King WG, Brugge JS, Symons M, Hynes RO: Integrin-mediated signals regulated by members of the rho family of GTPases. J Cell Biol 1998, 142:573-586.
    • (1998) J Cell Biol , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 22
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • Takaishi K, Sasaki T, Kotani H, Nishioka H, Takai Y: Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J Cell Biol 1997, 139:1047-1059.
    • (1997) J Cell Biol , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 23
    • 0030904698 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion by the small GTP-binding protein Rho in small cell lung carcinoma cells
    • Tokman MG, Porter RA, Williams CL: Regulation of cadherin-mediated adhesion by the small GTP-binding protein Rho in small cell lung carcinoma cells. Cancer Res 1997, 57:1785-1793.
    • (1997) Cancer Res , vol.57 , pp. 1785-1793
    • Tokman, M.G.1    Porter, R.A.2    Williams, C.L.3
  • 24
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga VM, Machesky LM, Hall A, Hotchin NA: The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J Cell Biol 1997, 137:1421-1431.
    • (1997) J Cell Biol , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 25
    • 2642615752 scopus 로고    scopus 로고
    • Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endothelial cells
    • Wojciak-Stothard B, Entwistle A, Garg R, Ridley AJ: Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endothelial cells. J Cell Physiol 1998, 176:150-165.
    • (1998) J Cell Physiol , vol.176 , pp. 150-165
    • Wojciak-Stothard, B.1    Entwistle, A.2    Garg, R.3    Ridley, A.J.4
  • 26
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C, Chrzanowska-Wodnicka M, Brown J, Shaub A, Belkin AM, Burridge K: Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J Cell Biol 1998, 141:539-551.
    • (1998) J Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 27
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction
    • Zhang Q, Magnusson MK, Mosher DF: Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction. Mol Biol Cell 1997, 8:1415-1425.
    • (1997) Mol Biol Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.K.2    Mosher, D.F.3
  • 29
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/ radixin/ moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S, Tsukita S: Rho-kinase phosphorylates COOH-terminal threonines of ezrin/ radixin/ moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol 1998, 140:647-657.
    • (1998) J Cell Biol , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7    Tsukita, S.8
  • 30
    • 0030293886 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/ Rho-dependent effector pathways
    • Reif K, Nobes CD, Thomas G, Hall A, Cantrell DA: Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/ Rho-dependent effector pathways. Curr Biol 1996, 6:1445-1455.
    • (1996) Curr Biol , vol.6 , pp. 1445-1455
    • Reif, K.1    Nobes, C.D.2    Thomas, G.3    Hall, A.4    Cantrell, D.A.5
  • 31
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways
    • Westwick JK, Lambert QT, Clark GJ, Symons M, Van Aelst L, Pestell RG, Der CJ: Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol Cell Biol 1997, 17:1324-1335.
    • (1997) Mol Cell Biol , vol.17 , pp. 1324-1335
    • Westwick, J.K.1    Lambert, Q.T.2    Clark, G.J.3    Symons, M.4    Van Aelst, L.5    Pestell, R.G.6    Der, C.J.7
  • 32
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill CS, Wynne J, Treisman R: The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 1995, 81:1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3


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