메뉴 건너뛰기




Volumn 147, Issue 5, 1999, Pages 1023-1037

Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo

Author keywords

Cytokinesis; Myosin binding subunit of myosin phosphatase; Phosphorylation; Rho; Rho associated kinase

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE; PROTEIN SUBUNIT; RHO FACTOR;

EID: 0033615977     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.5.1023     Document Type: Article
Times cited : (486)

References (85)
  • 1
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targeting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi, D., L.K. MacDougall, M.M. Sola, M. Ikebe, and P. Cohen. 1992. The control of protein phosphatase-1 by targeting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210:1023-1035.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 7
    • 0032561312 scopus 로고    scopus 로고
    • Modification of the E-cadherin-catenin complex in mitotic Madin-Darhy canine kidney epithelial cells
    • Bauer, A., H. Lickert, R. Kemler, and J. Stappert. 1998. Modification of the E-cadherin-catenin complex in mitotic Madin-Darhy canine kidney epithelial cells. J. Biol. Chem. 273:28314-28321.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28314-28321
    • Bauer, A.1    Lickert, H.2    Kemler, R.3    Stappert, J.4
  • 8
    • 0028822081 scopus 로고
    • Phosphorylation on threonine-18 of the regulatory light chain dissociates the ATP-ase and motor properties of smooth muscle myosin II
    • Bresnick, A.R., V.L. Wolff-Long, O. Baumann, and T.D. Pollard. 1995. Phosphorylation on threonine-18 of the regulatory light chain dissociates the ATP-ase and motor properties of smooth muscle myosin II. Biochemistry,34: 12576-12583.
    • (1995) Biochemistry , vol.34 , pp. 12576-12583
    • Bresnick, A.R.1    Wolff-Long, V.L.2    Baumann, O.3    Pollard, T.D.4
  • 9
    • 0032511197 scopus 로고    scopus 로고
    • The small GTP-binding protein Rhoa regulates a delayed rectifier potassium channel
    • Cachero, T.G., A.D. Morielli, and E.G. Peralta. 1998. The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. Cell. 93:1077-1085.
    • (1998) Cell , vol.93 , pp. 1077-1085
    • Cachero, T.G.1    Morielli, A.D.2    Peralta, E.G.3
  • 10
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of erk- and rsk-encoded protein kinases
    • Chen, R.H., C. Sarnecki, and J. Blenis. 1992. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol. Cell Biol. 12:915-927.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 915-927
    • Chen, R.H.1    Sarnecki, C.2    Blenis, J.3
  • 12
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper, J.A. 1991. The role of actin polymerization in cell motility. Annu. Rev. Physiol. 53:585-605.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 13
    • 0023684217 scopus 로고
    • Changes in fibroblast contractility, morphology, and adhesion in response to a phorbol ester tumor promoter
    • Danowski, B.A., and A.K. Harris. 1988. Changes in fibroblast contractility, morphology, and adhesion in response to a phorbol ester tumor promoter. Exp. Cell Res. 177:47-59.
    • (1988) Exp. Cell Res. , vol.177 , pp. 47-59
    • Danowski, B.A.1    Harris, A.K.2
  • 14
    • 0032555506 scopus 로고    scopus 로고
    • Thrombin inactivates myosin light chain phosphatase via Rho and its target Rho kinase in human endothelial cells
    • Essler, M., M. Amano, H.J. Kruse, K. Kaibuchi, P.C. Weber, and M. Aepfelbacher. 1998. Thrombin inactivates myosin light chain phosphatase via Rho and its target Rho kinase in human endothelial cells. J. Biol. Chem. 272: 21867-21874.
    • (1998) J. Biol. Chem. , vol.272 , pp. 21867-21874
    • Essler, M.1    Amano, M.2    Kruse, H.J.3    Kaibuchi, K.4    Weber, P.C.5    Aepfelbacher, M.6
  • 15
    • 0032550225 scopus 로고    scopus 로고
    • Association of the myosin-binding subunit of myosin phosphatase and moesin: Dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase
    • Fukata, Y., K. Kimura, N. Oshiro, H. Saya, Y. Matsuura, and K. Kaibuchi. 1998. Association of the myosin-binding subunit of myosin phosphatase and moesin: dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase. J. Cell Biol. 141:409-418.
    • (1998) J. Cell Biol. , vol.141 , pp. 409-418
    • Fukata, Y.1    Kimura, K.2    Oshiro, N.3    Saya, H.4    Matsuura, Y.5    Kaibuchi, K.6
  • 18
    • 0032496146 scopus 로고    scopus 로고
    • Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis
    • Goto, H., H. Kosako, K. Tanabe, M. Yanagida, M. Sakurai, M. Amano, K. Kaibuchi, and M. Inagaki. 1998. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J. Biol. Chem. 273:11728-11736.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11728-11736
    • Goto, H.1    Kosako, H.2    Tanabe, K.3    Yanagida, M.4    Sakurai, M.5    Amano, M.6    Kaibuchi, K.7    Inagaki, M.8
  • 19
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science. 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 20
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne, D.J., M. Ito, and F. Erdodi. 1998. Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19:325-341.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 21
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and Cdc42Hs regulate transcriptional activation by SRF
    • Hill, C.S., J. Wynne, and R. Treisman. 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
  • 24
    • 0029976102 scopus 로고    scopus 로고
    • Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity
    • Ichikawa, K., M. Ito, and D.J. Hartshorne. 1996. Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity. J. Biol. Chem. 271:4733-4740.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4733-4740
    • Ichikawa, K.1    Ito, M.2    Hartshorne, D.J.3
  • 25
    • 0031002831 scopus 로고    scopus 로고
    • Phosphorylation-dependent control of structures of intermediate filaments: A novel approach using site- and phosphorylation state-specific antibodies
    • Inagaki, M., N. Inagaki, T. Takahashi, and Y. Takai. 1997. Phosphorylation-dependent control of structures of intermediate filaments: a novel approach using site- and phosphorylation state-specific antibodies. J. Biochem. 121:407-414.
    • (1997) J. Biochem. , vol.121 , pp. 407-414
    • Inagaki, M.1    Inagaki, N.2    Takahashi, T.3    Takai, Y.4
  • 28
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki, T., M. Naito, K. Fujisawa, M. Maekawa, N. Watanabe, Y. Saito, and S. Narumiya. 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
  • 30
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- And thrombin-induced neurite retraction and neuronal cell rounding by ADP rihosylation of the small GTP-binding protein Rho
    • Jalink, K., E.J. van Corven, T. Hengeveld, N. Morii, S. Narumiya, and W.H. Moolenaar. 1994. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP rihosylation of the small GTP-binding protein Rho. J. Cell Biol. 126:801-810.
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 31
    • 0030615319 scopus 로고    scopus 로고
    • Identification of the regions on the M110 subunit of protein phosphatase 1M that interact with the M21 subunit and with myosin
    • Johnson, D., P. Cohen, M.X. Chen, Y.H. Chen, and P.T. Cohen. 1997. Identification of the regions on the M110 subunit of protein phosphatase 1M that interact with the M21 subunit and with myosin. Eur. J. Biochem. 244:931-993.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 931-993
    • Johnson, D.1    Cohen, P.2    Chen, M.X.3    Chen, Y.H.4    Cohen, P.T.5
  • 32
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • Kaibuchi, K., S. Kuroda, and M. Amano. 1999. Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem. 68:459-486.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 33
    • 0028009358 scopus 로고
    • Mutagenesis of the phosphorylation site (serine 19) of smooth muscle myosin regulatory light chain and its effects on the properties of myosin
    • Kamisoyama, H., Y. Araki, and M. Ikebe. 1994. Mutagenesis of the phosphorylation site (serine 19) of smooth muscle myosin regulatory light chain and its effects on the properties of myosin. Biochemistry, 33:840-847.
    • (1994) Biochemistry , vol.33 , pp. 840-847
    • Kamisoyama, H.1    Araki, Y.2    Ikebe, M.3
  • 35
    • 0032579378 scopus 로고    scopus 로고
    • p 160 RhoA-binding kinase ROKu induces neurite retraction
    • Katoh, H., J. Aoki, A. Ichikawa, and M. Negishi. 1998. p 160 RhoA-binding kinase ROKu induces neurite retraction. J. Biol. Chem. 273:2489-2492.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2489-2492
    • Katoh, H.1    Aoki, J.2    Ichikawa, A.3    Negishi, M.4
  • 37
    • 0032489531 scopus 로고    scopus 로고
    • Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase
    • Kimura, K., Y. Fukata, Y. Matsuoka, V. Bennett, Y. Matsuura, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1998. Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase. J. Biol. Chem. 273:5542-5548.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5542-5548
    • Kimura, K.1    Fukata, Y.2    Matsuoka, Y.3    Bennett, V.4    Matsuura, Y.5    Okawa, K.6    Iwamatsu, A.7    Kaibuchi, K.8
  • 38
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • Kishi, K., T. Sasaki, S. Kuroda, T. Itoh, and Y. Takai. 1993. 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) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 40
    • 0030929849 scopus 로고    scopus 로고
    • Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase
    • Kosako, H., M. Amano, M. Yanagida, K. Tanabe, Y. Nishi, K. Kaibuchi, and M. Inagaki. 1997. Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase. J. Biol. Chem. 272:10333-10336.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10333-10336
    • Kosako, H.1    Amano, M.2    Yanagida, M.3    Tanabe, K.4    Nishi, Y.5    Kaibuchi, K.6    Inagaki, M.7
  • 41
    • 0033614371 scopus 로고    scopus 로고
    • Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: Cleavage furrow-specific phosphorylation of intermediate filament
    • Kosako, U., H. Goto, M. Yanagida, K. Matsuzawa, Y. Tomono, T. Okigaki, H. Odai, K. Kaibuchi, and M. Inagaki. 1999. Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filament. Oncogene. 18:2783-2788.
    • (1999) Oncogene , vol.18 , pp. 2783-2788
    • Kosako, U.1    Goto, H.2    Yanagida, M.3    Matsuzawa, K.4    Tomono, Y.5    Okigaki, T.6    Odai, H.7    Kaibuchi, K.8    Inagaki, M.9
  • 42
    • 0030977123 scopus 로고    scopus 로고
    • Rho-associated kinase directly induces smooth muscle contraction through myosin lighl chain phosphorylation
    • Kureishi, Y., S. Kobayashi, M. Amano, K. Kimura, H. Kanaide, T. Nakano, K. Kaibuchi, and M. Ito. 1997. Rho-associated kinase directly induces smooth muscle contraction through myosin lighl chain phosphorylation. J. Biol. Chem. 272:12257-12260.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12257-12260
    • Kureishi, Y.1    Kobayashi, S.2    Amano, M.3    Kimura, K.4    Kanaide, H.5    Nakano, T.6    Kaibuchi, K.7    Ito, M.8
  • 43
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D.A., and A.F. Horwitz. 1996. Cell migration: a physically integrated molecular process. Cell. 84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 44
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., F. Manser, L. Tan, and L. Lim. 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, F.2    Tan, L.3    Lim, L.4
  • 45
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROKu is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., X.Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROKu 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
  • 46
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi, I., Y. Hamaguchi, H. Fujimoto, N. Morii, M. Mishima, and S. Narumiya. 1993. A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote, 1:325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 50
    • 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., M. Maeda, Y. Doi, S. Yonemura, M. Amano, K. Kaibuchi, S. Tsukita, and S. Tsukita. 1998. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 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
  • 51
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells
    • Matsumura, F., S. Ono, Y. Yamakita, G. Totsukawa, and S. Yamashiro. 1998. Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140:119-129.
    • (1998) J. Cell Biol. , vol.140 , pp. 119-129
    • Matsumura, F.1    Ono, S.2    Yamakita, Y.3    Totsukawa, G.4    Yamashiro, S.5
  • 52
    • 0023091932 scopus 로고
    • Baculovirus expression vectors: The requirements for high level expression of proteins, including glycoproteins
    • Matsuura, Y., R.D. Possee, H.A. Overton, and D.H. Bishop. 1987. Baculovirus expression vectors: the requirements for high level expression of proteins, including glycoproteins. J. Gen. Virol. 68:1233-1250.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1233-1250
    • Matsuura, Y.1    Possee, R.D.2    Overton, H.A.3    Bishop, D.H.4
  • 53
    • 0030049170 scopus 로고    scopus 로고
    • Actin-hased cell motility and cell locomotion
    • Mitchison, T.J., and L.P. Cramer. 1996. Actin-hased cell motility and cell locomotion. Cell. 84:371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 54
    • 0023198109 scopus 로고
    • Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene
    • Montminy, M.R., and L.M. Bilevikjian. 1987. Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene. Nature. 328: 175-178.
    • (1987) Nature , vol.328 , pp. 175-178
    • Montminy, M.R.1    Bilevikjian, L.M.2
  • 55
    • 0029147540 scopus 로고
    • Preparation of native and recombinant Clostridium botulinum C3 ADP-ribosyltransferase and identification of Rho proteins by ADP-rihosylation
    • Morii, N., and S. Narumiya. 1995. Preparation of native and recombinant Clostridium botulinum C3 ADP-ribosyltransferase and identification of Rho proteins by ADP-rihosylation. Methods Enzymol. 256:196-206.
    • (1995) Methods Enzymol. , vol.256 , pp. 196-206
    • Morii, N.1    Narumiya, S.2
  • 56
    • 0031004803 scopus 로고    scopus 로고
    • Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts
    • Murata, K., K. Hirano, E. Villa-Moruzzi, D.J. Hartshorne, and D.L. Brautigan. 1997. Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts. Mol. Biol. Cell. 8:663-673.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 663-673
    • Murata, K.1    Hirano, K.2    Villa-Moruzzi, E.3    Hartshorne, D.J.4    Brautigan, D.L.5
  • 57
    • 0023225108 scopus 로고
    • Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA
    • Nagafuchi, A., Y. Shirayoshi, K. Okazaki, K. Yasuda, and M. Takeichi. 1987. Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA. Nature. 329:341-343.
    • (1987) Nature , vol.329 , pp. 341-343
    • Nagafuchi, A.1    Shirayoshi, Y.2    Okazaki, K.3    Yasuda, K.4    Takeichi, M.5
  • 58
  • 60
    • 0025233512 scopus 로고
    • ADP-ribosylation of the rho/rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells
    • Nishiki, T., S. Narumiya, N. Morii, M. Yamamoto, M. Fujiwara, Y. Kamata, G. Sakaguchi, and S. Kozaki. 1990. ADP-ribosylation of the rho/rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells. Biochem. Biophys. Res. Commun. 167:265-272.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 265-272
    • Nishiki, T.1    Narumiya, S.2    Morii, N.3    Yamamoto, M.4    Fujiwara, M.5    Kamata, Y.6    Sakaguchi, G.7    Kozaki, S.8
  • 61
    • 0028258943 scopus 로고
    • rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- And 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells
    • Nishiyama, T., T. Sasaki, K. Takaishi, M. Kato, H. Yaku, K. Araki, Y. Matsuura, and Y. Takai. 1994. rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. Mol. Cell. Biol. 14:2447-2456.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5    Araki, K.6    Matsuura, Y.7    Takai, Y.8
  • 62
    • 0028980248 scopus 로고
    • Involvement of rho in GTP gamma S-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: Inhibition of phosphatase activity
    • Noda, M., C. Yasuda-Fukazawa, K. Moriishi, T. Kato, T. Okuda, K. Kurokawa, and Y. Takuwa. 1995. Involvement of rho in GTP gamma S-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity. FEBS Lett. 367:246-250.
    • (1995) FEBS Lett. , vol.367 , pp. 246-250
    • Noda, M.1    Yasuda-Fukazawa, C.2    Moriishi, K.3    Kato, T.4    Okuda, T.5    Kurokawa, K.6    Takuwa, Y.7
  • 63
    • 0032567361 scopus 로고    scopus 로고
    • Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
    • Oshiro, N., Y. Fukata, and K. Kaibuchi. 1998. Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. J. Biol. Chem. 273:34663-34666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34663-34666
    • Oshiro, N.1    Fukata, Y.2    Kaibuchi, K.3
  • 64
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase. PKN, and rho-philin in the rho-binding domain
    • Reid, T., T. Furuyashiki, T. Ishizaki, G. Watanabe, N. Watanabe, K. Fujisawa, N. Morii, P. Madaule, and S. Narumiya. 1996. Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase. PKN, and rho-philin 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
  • 65
    • 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., and A. Hall. 1992. 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) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 66
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., H.F. Paterson, C.L. Johnston, D. Diekmann, and A. Hall. 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, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 67
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fiber formation: Requirement for a tyrosine kinase
    • Ridley, A.J., and A. Hall. 1994. Signal transduction pathways regulating Rho-mediated stress fiber formation: requirement for a tyrosine kinase. EMBO (Eur. Mol. Biol. Organ.) J. 13:2600-2610.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 68
    • 0025736018 scopus 로고
    • Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis
    • Sato, N., S. Yonemura, T. Obinata, S. Tsukita, and S. Tsukita. 1991. Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis. J. Cell Biol. 113:321-330.
    • (1991) J. Cell Biol. , vol.113 , pp. 321-330
    • Sato, N.1    Yonemura, S.2    Obinata, T.3    Tsukita, S.4    Tsukita, S.5
  • 70
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R.J., M. Henry, F. Solomon, and T. Jacks. 1998. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell. 9:403-419.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 72
    • 0030907067 scopus 로고    scopus 로고
    • Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D
    • Singer, W.D., H.A. Brown, and P.C. Sternweis. 1997. Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D. Annu. Rev. Biochem. 66:475-509.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 475-509
    • Singer, W.D.1    Brown, H.A.2    Sternweis, P.C.3
  • 73
    • 0030657895 scopus 로고    scopus 로고
    • Rhomantic interludes raise blood pressure
    • Sumlyo, A. 1997. Rhomantic interludes raise blood pressure. Nature. 389:908-911.
    • (1997) Nature , vol.389 , pp. 908-911
    • Sumlyo, A.1
  • 74
    • 0028118847 scopus 로고
    • Charge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation
    • Sweeney, H.L., Z. Yang, G. Zhi, J.T. Stull, and K.M. Trybus. 1994. Charge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation. Proc. Natl. Acad. Sci. USA. 91: 1490-1494.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1490-1494
    • Sweeney, H.L.1    Yang, Z.2    Zhi, G.3    Stull, J.T.4    Trybus, K.M.5
  • 75
    • 0027391509 scopus 로고
    • Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility
    • Takaishi, K., A. Kikuchi, S. Kuroda, K. Kotani, T. Sasaki, and Y. Takai. 1993. Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility. Mol. Cell. Biol. 13:72-79.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 72-79
    • Takaishi, K.1    Kikuchi, A.2    Kuroda, S.3    Kotani, K.4    Sasaki, T.5    Takai, Y.6
  • 76
    • 0027952703 scopus 로고
    • Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility
    • Takaishi, K., T. Sasaki, M. Kato, W. Yamochi, S. Kuroda, T. Nakamura, M. Takeichi, and Y. Takai. 1994. Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility. Oncogene. 9:273-279.
    • (1994) Oncogene , vol.9 , pp. 273-279
    • Takaishi, K.1    Sasaki, T.2    Kato, M.3    Yamochi, W.4    Kuroda, S.5    Nakamura, T.6    Takeichi, M.7    Takai, Y.8
  • 77
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi, K., T. Sasaki, T. Kameyama, S. Tsukita, S. Tsukita, and Y. Takai. 1995. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Tsukita, S.5    Takai, Y.6
  • 78
    • 0029132694 scopus 로고
    • Thiophosphorylation of the 130-kDa subunit is associated with a decreased activity of myosin light chain phosphatase in alpha-toxin-permeabilized smooth muscle
    • Trinkle-Mulcahy, L., K. Ichikawa, D.J. Hartshorne, M.J. Siegman, and T.M. Butler. 1995. Thiophosphorylation of the 130-kDa subunit is associated with a decreased activity of myosin light chain phosphatase in alpha-toxin-permeabilized smooth muscle. J. Biol. Chem. 270:18191-18194.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18191-18194
    • Trinkle-Mulcahy, L.1    Ichikawa, K.2    Hartshorne, D.J.3    Siegman, M.J.4    Butler, T.M.5
  • 79
    • 0025295180 scopus 로고
    • Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding
    • Ueda, T., A. Kikuchi, N. Ohga, J. Yamamoto, and Y. Takai. 1990. Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding. J. Biol. Chem. 265:9373-9380.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9373-9380
    • Ueda, T.1    Kikuchi, A.2    Ohga, N.3    Yamamoto, J.4    Takai, Y.5
  • 81
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 84
    • 0025834881 scopus 로고
    • An increase or a decrease in myosin II phosphorylation inhibits macrophage motility
    • Wilson, A.K., G. Gorgas, W.D. Claypool, and P. de Lanerolle. 1991. An increase or a decrease in myosin II phosphorylation inhibits macrophage motility. J. Cell Biol. 114:277-283.
    • (1991) J. Cell Biol. , vol.114 , pp. 277-283
    • Wilson, A.K.1    Gorgas, G.2    Claypool, W.D.3    De Lanerolle, P.4
  • 85
    • 0032583123 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase (Rho-kinase) in cytokinesis; mutations in Rho-kinase phosphorylation sites impair cytokinetic segregation of glial filaments
    • Yasui, Y., M. Amano, N. Inagaki, K. Nagata, H. Nakamura, H. Saya, K. Kaibuchi, and M. Inagaki. 1998. Roles of Rho-associated kinase (Rho-kinase) in cytokinesis; mutations in Rho-kinase phosphorylation sites impair cytokinetic segregation of glial filaments. J. Cell Biol. 143:1249-1258.
    • (1998) J. Cell Biol. , vol.143 , pp. 1249-1258
    • Yasui, Y.1    Amano, M.2    Inagaki, N.3    Nagata, K.4    Nakamura, H.5    Saya, H.6    Kaibuchi, K.7    Inagaki, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.