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Volumn 1, Issue 3, 1999, Pages 136-143

Cooperation between mDia1 and ROCK in Rho-induced actin reorganization

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CARRIER PROTEIN; GUANOSINE TRIPHOSPHATE; PROTEIN SERINE THREONINE KINASE; RECOMBINANT PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHO KINASE; RHO-ASSOCIATED KINASE; SIGNAL PEPTIDE;

EID: 0033160196     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/11056     Document Type: Article
Times cited : (743)

References (42)
  • 1
    • 0030612748 scopus 로고    scopus 로고
    • Rho effectors and reorganization of actin cytoskeleton
    • Narumiya, S., Ishizaki, T. & Watanabe, N. Rho effectors and reorganization of actin cytoskeleton. FEBS Lett. 410, 68-72 (1997).
    • (1997) FEBS Lett. , vol.410 , pp. 68-72
    • Narumiya, S.1    Ishizaki, T.2    Watanabe, N.3
  • 2
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509-514 (1998).
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 3
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21rho induces rapid changes in cell morphology
    • Paterson, H. F. et al. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 1001-1007
    • Paterson, H.F.1
  • 4
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J. & Hall, A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399 (1992).
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 5
    • 0028894787 scopus 로고
    • Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells
    • Ridley, A. J., Comoglio, P. M. & Hall, A. Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells. Mol. Cell Biol. 15, 1110-1122 (1995).
    • (1995) Mol. Cell Biol. , vol.15 , pp. 1110-1122
    • Ridley, A.J.1    Comoglio, P.M.2    Hall, A.3
  • 6
    • 0030615004 scopus 로고    scopus 로고
    • S. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki, T. et al. S. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett. 404, 118-124 (1997).
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1
  • 7
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • Kishi, K., Sasaki, T., Kuroda, S., Itoh, T. & Takai, Y. Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J. Cell Biol. 120, 1187-1195 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 8
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi, I. et al. A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote 1, 325-331 (1993).
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1
  • 9
    • 0031037187 scopus 로고    scopus 로고
    • A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
    • Drechsel, D. N., Hyman, A. A., Hall, A. & Glotzer, M. A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr. Biol. 7, 12-23 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 12-23
    • Drechsel, D.N.1    Hyman, A.A.2    Hall, A.3    Glotzer, M.4
  • 10
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites & cleavage furrows
    • Takaishi, K. et al. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites & cleavage furrows. Oncogene 11, 39-48 (1995).
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1
  • 11
    • 0030015626 scopus 로고    scopus 로고
    • Rho-dependent membrane folding causes Shigella entry into epithelial cells
    • Adam, T., Giry, M., Boquet, P. & Sansonetti, P. Rho-dependent membrane folding causes Shigella entry into epithelial cells. EMBO J. 15, 3315-3321 (1996).
    • (1996) EMBO J. , vol.15 , pp. 3315-3321
    • Adam, T.1    Giry, M.2    Boquet, P.3    Sansonetti, P.4
  • 12
    • 0030032067 scopus 로고    scopus 로고
    • The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells
    • Menard, R., Prevost, M. C., Gounon, P., Sansonetti, P. & Dehio, C. The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells. Proc. Natl Acad. Sci. USA 93, 1254-1258 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1254-1258
    • Menard, R.1    Prevost, M.C.2    Gounon, P.3    Sansonetti, P.4    Dehio, C.5
  • 13
    • 0031052018 scopus 로고    scopus 로고
    • Rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells
    • Watarai, M., Kamata, Y., Kozaki, S. & Sasakawa, C. rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells. J. Exp. Med. 185, 281-292 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 281-292
    • Watarai, M.1    Kamata, Y.2    Kozaki, S.3    Sasakawa, C.4
  • 14
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine, A., Fujiwara, M. & Narumiya, S. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 15
    • 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. 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).
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 16
    • 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. & 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. 16, 5313-5327 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 17
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • Amano, M. et al. Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 275, 1308-1311 (1997).
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1
  • 18
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura, K. et al. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 273, 245-248 (1996).
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1
  • 19
    • 0030657895 scopus 로고    scopus 로고
    • Rhomantic interludes raise blood pressure
    • Somlyo, A.P. Rhomantic interludes raise blood pressure. Nature 389, 908-911 (1997).
    • (1997) Nature , vol.389 , pp. 908-911
    • Somlyo, A.P.1
  • 20
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
    • Uehata, M. et al. Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature 389, 990-994 (1997).
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1
  • 21
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • Castrillon, D. H. & Wasserman, S. A. Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120, 3367-3377 (1994).
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 22
    • 0031194074 scopus 로고    scopus 로고
    • Actin cytoskeleton: Are FH proteins local organizers?
    • Frazier, J. A. & Field, C. M. Actin cytoskeleton: are FH proteins local organizers? Curr. Biol. 7, R414-R417 (1997).
    • (1997) Curr. Biol. , vol.7
    • Frazier, J.A.1    Field, C.M.2
  • 23
    • 0032031388 scopus 로고    scopus 로고
    • FH proteins as cytoskeletal organizers
    • Wasserman, S. FH proteins as cytoskeletal organizers. Trends Cell Biol. 8, 111-115 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 111-115
    • Wasserman, S.1
  • 24
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier, M. F. & Pantaloni, D. Control of actin dynamics in cell motility. J. Mol. Biol. 269, 459-467 (1997).
    • (1997) J. Mol. Biol. , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 26
    • 0030707797 scopus 로고    scopus 로고
    • Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous
    • Lynch, E. D. et al. Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous. Science 278, 1315-1318 (1997).
    • (1997) Science , vol.278 , pp. 1315-1318
    • Lynch, E.D.1
  • 27
    • 0032581530 scopus 로고    scopus 로고
    • Role of citron kinase as a target of the small GTPase Rho in cytokinesis
    • Madaule, P. et al. Role of citron kinase as a target of the small GTPase Rho in cytokinesis. Nature 394, 491-494 (1998).
    • (1998) Nature , vol.394 , pp. 491-494
    • Madaule, P.1
  • 28
    • 14444288533 scopus 로고    scopus 로고
    • Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells
    • Hirose, M. et al. Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells. J. Cell Biol. 141, 1625-1636 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1625-1636
    • Hirose, M.1
  • 29
    • 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
    • Alberts, A. S., Bouquin, N., Johnston, L. H. & Treisman, R. 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, 8616-8622 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 30
    • 0032473351 scopus 로고    scopus 로고
    • RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation
    • Sahai, E., Alberts, A. S. & Treisman, R. RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 17, 1350-1361 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1350-1361
    • Sahai, E.1    Alberts, A.S.2    Treisman, R.3
  • 31
    • 10544228528 scopus 로고    scopus 로고
    • Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • Kohno, H. et al. Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15, 6060-6068 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6060-6068
    • Kohno, H.1
  • 32
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista, M. et al. Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122 (1997).
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1
  • 33
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- And thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink, K. et al. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J. Cell Biol. 126, 801-810 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1
  • 34
    • 0029833287 scopus 로고    scopus 로고
    • Genetic evidence that formins function within the nucleus
    • Chan, D. C. & Leder, P. Genetic evidence that formins function within the nucleus. J. Biol. Chem. 271, 23472-23477 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 23472-23477
    • Chan, D.C.1    Leder, P.2
  • 35
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke, W. et al. In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. EMBO J. 17, 967-976 (1998).
    • (1998) EMBO J. , vol.17 , pp. 967-976
    • Witke, W.1
  • 36
    • 0031665143 scopus 로고    scopus 로고
    • Rho1p-Bni1p-Spa2p interactions: Implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae
    • Fujiwara, T. et al. Rho1p-Bni1p-Spa2p interactions: implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Biol. Cell 9, 1221-1233 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1221-1233
    • Fujiwara, T.1
  • 37
    • 0032537023 scopus 로고    scopus 로고
    • Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: Implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Umikawa, M. et al. Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene 16, 2011-2016 (1998).
    • (1998) Oncogene , vol.16 , pp. 2011-2016
    • Umikawa, M.1
  • 38
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation
    • Petersen, J., Nielsen, O., Egel, R. & Hagan, I. M. FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J. Cell Biol. 141, 1217-1228 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1217-1228
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, I.M.4
  • 39
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki, H., Sasaki, T., Takai, Y. & Takenawa, T. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391, 93-96 (1998).
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 40
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization
    • Machesky, L. M. & Hall, A. Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization. J. Cell Biol. 138, 913-926 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 41
    • 0025007616 scopus 로고
    • 'Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik, R.P., Maas, R.L., Zeller, R., Vogt, T.F. & Leder, P. 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Nature 346, 850-553 (1990).
    • (1990) Nature , vol.346 , pp. 850-1553
    • Woychik, R.P.1    Maas, R.L.2    Zeller, R.3    Vogt, T.F.4    Leder, P.5
  • 42
    • 17344369363 scopus 로고    scopus 로고
    • A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: Evidence for conserved function in oogenesis and implications for human sterility
    • Bione, S. et al. A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: evidence for conserved function in oogenesis and implications for human sterility. Am. J. Hum. Genet. 62, 533-541 (1998).
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 533-541
    • Bione, S.1


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