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Volumn 17, Issue 5, 1998, Pages 1350-1361

RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation

Author keywords

Cytoskeleton; PKN; RhoA; ROCK; Serum response element; SRF; Transformation

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; PROTEIN KINASE; RAS PROTEIN; RHO FACTOR; SERUM RESPONSE FACTOR; UNCLASSIFIED DRUG;

EID: 0032473351     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.5.1350     Document Type: Article
Times cited : (233)

References (54)
  • 1
    • 0032549013 scopus 로고    scopus 로고
    • Activation of SRF-regulated chromosomal templates by Rho-family GTPases requires a signal that also induces H4 hyperacetylation
    • in press
    • Alberts, A., Geneste, O. and Treisman, R. (1998a) Activation of SRF-regulated chromosomal templates by Rho-family GTPases requires a signal that also induces H4 hyperacetylation. Cell, 92, in press.
    • (1998) Cell , vol.92
    • Alberts, A.1    Geneste, O.2    Treisman, R.3
  • 2
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7
    • in press
    • Alberts, A.S., Bouquin, N., Johnston, L.H. and Treisman, R.H. (1998b) Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J. Biol. Chem., 273, in press.
    • (1998) J. Biol. Chem. , vol.273
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.H.4
  • 7
    • 0029917989 scopus 로고    scopus 로고
    • Isolation of a novel oncogene, NET1, from neuroepithelioma cells by expression cDNA cloning
    • Chan, A.M., Takai, S., Yamada, K. and Miki, T. (1996) Isolation of a novel oncogene, NET1, from neuroepithelioma cells by expression cDNA cloning. Oncogene, 12, 1259-1126.
    • (1996) Oncogene , vol.12 , pp. 1259-11126
    • Chan, A.M.1    Takai, S.2    Yamada, K.3    Miki, T.4
  • 8
    • 15444360813 scopus 로고    scopus 로고
    • Cytoskeletal rearrangements and transe optional activation of c-fos serum response element by Rho-kinase
    • Chihara, K. et al. (1997) Cytoskeletal rearrangements and transe optional activation of c-fos serum response element by Rho-kinase. J. Biol. Chem., 272, 25121-25127.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25121-25127
    • Chihara, K.1
  • 9
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L.D., Traynor, K.A., Bokoch, G.M. and Schwartz, M.A. (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, K.A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 10
    • 0029814413 scopus 로고    scopus 로고
    • Rac 'insert region' is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65
    • Freeman, J.L., Abo, A. and Lambeth, J.D. (1996) Rac 'insert region' is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65. J. Biol. Chem., 271, 19794-19801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19794-19801
    • Freeman, J.L.1    Abo, A.2    Lambeth, J.D.3
  • 11
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill, C.S., Wynne, J. and Treisman, R. (1995) The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell, 81, 1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 12
    • 0031034136 scopus 로고    scopus 로고
    • The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue
    • Hirshberg, M., Stockley, R.W., Dodson, G. and Webb, M.R. (1997) The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat. Struct. Biol., 4, 147-152.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 147-152
    • Hirshberg, M.1    Stockley, R.W.2    Dodson, G.3    Webb, M.R.4
  • 13
    • 0030570801 scopus 로고    scopus 로고
    • Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor
    • Hotta, K., Tanaka, K., Mino, A., Kohno, H. and Takai, Y (1996) Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor. Biochem. Biophys. Res, Commun., 225, 69-74.
    • (1996) Biochem. Biophys. Res, Commun. , vol.225 , pp. 69-74
    • Hotta, K.1    Tanaka, K.2    Mino, A.3    Kohno, H.4    Takai, Y.5
  • 14
    • 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. and Narumiya, S. (1997) p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett., 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
  • 15
    • 0029802561 scopus 로고    scopus 로고
    • RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • Joneson, T., McDonough, M., Bar Sagi, D. and Van Aelst, L. (1996a) RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science, 274, 1374-1376.
    • (1996) Science , vol.274 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar Sagi, D.3    Van Aelst, L.4
  • 16
    • 0030052368 scopus 로고    scopus 로고
    • Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of RAS
    • Joneson, T., White, M.A., Wigler, M.H. and Bar Sagi, D. (1996b) Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of RAS. Science, 271, 810-812.
    • (1996) Science , vol.271 , pp. 810-812
    • Joneson, T.1    White, M.A.2    Wigler, M.H.3    Bar Sagi, D.4
  • 17
    • 0028800305 scopus 로고
    • Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
    • Khosravi-Far, R., Solski, P.A., Clark, G.J., Kinch, M.S. and Der, CJ. (1995) Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. Mol. Cell. Biol., 15, 6443-6453.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.J.3    Kinch, M.S.4    Der, C.J.5
  • 19
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura, K. et al. (1996) Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science, 273, 245-248.
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1
  • 21
    • 0030910236 scopus 로고    scopus 로고
    • Prenylation of RhoB is required for its cell transforming function but not its ability to activate serum response element-dependent transcription
    • Lebowitz, P.F, Du, W. and Prendergast, G.C. (1997) Prenylation of RhoB is required for its cell transforming function but not its ability to activate serum response element-dependent transcription. J. Biol. Chem., 212, 16093-16095.
    • (1997) J. Biol. Chem. , vol.212 , pp. 16093-16095
    • Lebowitz, P.F.1    Du, W.2    Prendergast, G.C.3
  • 22
    • 0026541143 scopus 로고
    • Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein
    • Leevers, S.J. and Marshall, C.J. (1992) Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein. EMBO J., 11, 569-574.
    • (1992) EMBO J. , vol.11 , pp. 569-574
    • Leevers, S.J.1    Marshall, C.J.2
  • 23
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., Manser, E., Tan, L. and Lim, L. (1995) A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem., 270, 29051-29054.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 24
    • 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, X.Q., Manser, E. and Lim, L. (1996) 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., 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
  • 25
    • 0029805324 scopus 로고    scopus 로고
    • Regulation of phosphorylation pathways by p21 GTPases. the p21 Ras-related Rho subfamily and its rote in phosphorylation signalling pathways
    • Lim, L., Manser, E., Leung, T. and Hall, C. (1996) Regulation of phosphorylation pathways by p21 GTPases. The p21 Ras-related Rho subfamily and its rote in phosphorylation signalling pathways. Eur. J. Biochem., 242, 171-185.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 171-185
    • Lim, L.1    Manser, E.2    Leung, T.3    Hall, C.4
  • 28
    • 9244257348 scopus 로고    scopus 로고
    • Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho
    • Matsui, T. et al. (1996) Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J., 15, 2208-2216.
    • (1996) EMBO J. , vol.15 , pp. 2208-2216
    • Matsui, T.1
  • 29
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protoncogenic ras proteins
    • Milburn, M.V., Tong, L., deVos, A.M., Brunger, A., Yamaizumi, Z., Nishimura, S. and Kim, S.H. (1990) Molecular switch for signal transduction: structural differences between active and inactive forms of protoncogenic ras proteins. Science, 247, 939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    Devos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 30
    • 0026632813 scopus 로고
    • Mutations of Ha-ras p21 that define important regions for the molecular mechanism of the SDC25 C-domain, a guanine nucleotide dissociation stimulator
    • Mistou, M.Y., Jacquet, E., Poullet, R, Rensland, H., Gideon, P., Schlichting, I., Wittinghofer, A. and Parmeggiani, A. (1992) Mutations of Ha-ras p21 that define important regions for the molecular mechanism of the SDC25 C-domain, a guanine nucleotide dissociation stimulator. EMBO J., 11, 2391-2397.
    • (1992) EMBO J. , vol.11 , pp. 2391-2397
    • Mistou, M.Y.1    Jacquet, E.2    Poullet, R.3    Rensland, H.4    Gideon, P.5    Schlichting, I.6    Wittinghofer, A.7    Parmeggiani, A.8
  • 31
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • Nakagawa, O., Fujisawa, K., Ishizaki, T., Saito, Y., Nakao, K. and Narumiya, S. (1996) ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett., 392, 189-193.
    • (1996) FEBS Lett. , vol.392 , pp. 189-193
    • Nakagawa, O.1    Fujisawa, K.2    Ishizaki, T.3    Saito, Y.4    Nakao, K.5    Narumiya, S.6
  • 32
    • 0030612748 scopus 로고    scopus 로고
    • Rho effectors and reorganization of actin cytoskeleton
    • Narumiya, S., Ishizaki, T. and Watanabe, N. (1997) Rho effectors and reorganization of actin cytoskeleton. FEBS Lett., 410, 68-72.
    • (1997) FEBS Lett. , vol.410 , pp. 68-72
    • Narumiya, S.1    Ishizaki, T.2    Watanabe, N.3
  • 33
    • 0030746214 scopus 로고    scopus 로고
    • Rac binding to p67(phox). Structural basis for interactions of the Rac1 effector region and insert region with components of the respiratory burst oxidase
    • Nisimoto, Y., Freeman, J.L.R., Motalebi, S.A., Hirshberg, M. and Lambeth, J.D. (1997) Rac binding to p67(phox). Structural basis for interactions of the Rac1 effector region and insert region with components of the respiratory burst oxidase. J. Biol. Chem., 272, 18834-18841.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18834-18841
    • Nisimoto, Y.1    Freeman, J.L.R.2    Motalebi, S.A.3    Hirshberg, M.4    Lambeth, J.D.5
  • 35
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • Pai, E.F., Kabsch, W., Krengel, U., HolmesK.C., John, J. and Wittinghofer, A. (1989) Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature, 341, 209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 36
    • 0027959781 scopus 로고
    • Identification of multiple, novel, protein kinase C-related gene products
    • Palmer, R.H., Ridden, J. and Parker, P.J. (1994) Identification of multiple, novel, protein kinase C-related gene products. FEBS Lett., 356, 5-8.
    • (1994) FEBS Lett. , vol.356 , pp. 5-8
    • Palmer, R.H.1    Ridden, J.2    Parker, P.J.3
  • 37
    • 0029091623 scopus 로고
    • Activation of PRK1 by phosphatidylinositol 4, 5-bisphosphate and phosphatidylinositol 3, 4, 5-trisphosphate. A comparison with protein kinase C isotypes
    • Palmer, R.H., Dekker, L.V., Woscholski, R., Le Good, J.A., Gigg, R. and Parker, P.J. (1995) Activation of PRK1 by phosphatidylinositol 4, 5-bisphosphate and phosphatidylinositol 3, 4, 5-trisphosphate. A comparison with protein kinase C isotypes. J. Biol. Chem., 270, 22412-22416.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22412-22416
    • Palmer, R.H.1    Dekker, L.V.2    Woscholski, R.3    Le Good, J.A.4    Gigg, R.5    Parker, P.J.6
  • 42
    • 10544241553 scopus 로고    scopus 로고
    • Isolation of a NCR-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling
    • Quilliam, L.A. et al (1996) Isolation of a NCR-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling. J. Biol. Chem., 271, 28772-28776.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28772-28776
    • Quilliam, L.A.1
  • 43
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the Rho-binding domain
    • Reid, T., Furuyashiki, T., Ishizaki, T., Watanabe, G., Watanabe, N., Fujisawa, K., Morii, N., Madaule, P. and Narumiya, S. (1996) Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the Rho-binding domain. J. Biol. Chem., 271, 13556-13560.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13556-13560
    • Reid, T.1    Furuyashiki, T.2    Ishizaki, T.3    Watanabe, G.4    Watanabe, N.5    Fujisawa, K.6    Morii, N.7    Madaule, P.8    Narumiya, S.9
  • 44
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren, X.D., Bokoch, G.M., Traynor-Kaplan, A., Jenkins, G.H., Anderson, R.A. and Schwartz, M.A. (1996) Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol. Biol. Cell, 7, 435-442.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 435-442
    • Ren, X.D.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.H.4    Anderson, R.A.5    Schwartz, M.A.6
  • 46
    • 0031004866 scopus 로고    scopus 로고
    • Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo
    • Shibasaki, Y., Ishihara, H., Kizuki, N., Asano, T., Oka, Y. and Yazaki, Y. (1997) Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo. J. Biol. Chem., 272, 7578-7581.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7578-7581
    • Shibasaki, Y.1    Ishihara, H.2    Kizuki, N.3    Asano, T.4    Oka, Y.5    Yazaki, Y.6
  • 47
    • 0030656619 scopus 로고    scopus 로고
    • + + sensitization of smooth muscle in hypertension
    • + + sensitization of smooth muscle in hypertension. Nature, 389, 990-994.
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1
  • 48
    • 0030894714 scopus 로고    scopus 로고
    • The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization
    • Vincent, S. and SettlemanJ, . (1997) The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol Cell. Biol., 17, 2247-2256.
    • (1997) Mol Cell. Biol. , vol.17 , pp. 2247-2256
    • Vincent, S.1    Settleman, J.2
  • 49
    • 13344285358 scopus 로고    scopus 로고
    • Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho
    • Watanabe, G. et al. (1996) Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science, 271, 645-648.
    • (1996) Science , vol.271 , pp. 645-648
    • Watanabe, G.1
  • 50
    • 0030911424 scopus 로고    scopus 로고
    • P140mDia. A mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe, N. et al (1997) p140mDia. a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin, EMBO J., 16, 3044-3056.
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 51
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways
    • Westwick, J.K., Lambert, Q.T., Ciark, G.J., Symons, M., Van Aelst, L., Pestell, R.G. and Der, C.J. (1997) Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol., 17, 1324-1335.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1324-1335
    • Westwick, J.K.1    Lambert, Q.T.2    Ciark, G.J.3    Symons, M.4    Van Aelst, L.5    Pestell, R.G.6    Der, C.J.7
  • 54
    • 0027280575 scopus 로고
    • ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle
    • Yamamoto, M, Marui, N., Sakai, T, Morii, N., Kozaki, S., Ikai, K., Imamura, S. and Narumiya, S. (1993) ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle. Oncogene, 8, 1449-1455.
    • (1993) Oncogene , vol.8 , pp. 1449-1455
    • Yamamoto, M.1    Marui, N.2    Sakai, T.3    Morii, N.4    Kozaki, S.5    Ikai, K.6    Imamura, S.7    Narumiya, S.8


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