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Volumn 7, Issue 3, 2005, Pages 255-261

Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOTONIC DYSTROPHY PROTEIN KINASE; PROTEIN CDC42; RHO FACTOR; RHO KINASE;

EID: 14744304060     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1230     Document Type: Article
Times cited : (329)

References (30)
  • 1
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A. & Horwitz, A. F. Cell migration: a physically integrated molecular process. Cell 84, 359-369 (1996).
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 2
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou, M. & Hall, A. Cell migration: Rho GTPases lead the way. Dev. Biol. 265, 23-32 (2004).
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 3
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: Mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • Wolf, K. et al. Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J. Cell Biol. 160, 267-277 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 267-277
    • Wolf, K.1
  • 4
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escape mechanisms
    • Friedl, P. & Wolf, K. Tumour-cell invasion and migration: diversity and escape mechanisms. Nature Rev. Cancer 3, 362-374 (2003).
    • (2003) Nature Rev. Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 5
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • Sahai, E. & Marshall, C. J. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nature Cell Biol. 5, 711-719 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 6
    • 9244220646 scopus 로고    scopus 로고
    • The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase
    • Ishizaki, T. et al. The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 15, 1885-1893 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1885-1893
    • Ishizaki, T.1
  • 7
    • 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
  • 8
    • 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. Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J. 15, 2208-2216 (1996).
    • (1996) EMBO J. , vol.15 , pp. 2208-2216
    • Matsui, T.1
  • 9
    • 0031962372 scopus 로고    scopus 로고
    • Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization
    • Leung, T., Chen, X. Q., Tan, I., Manser, E. & Lim, L. Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Mol. Cell. Biol. 18, 130-140 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 130-140
    • Leung, T.1    Chen, X.Q.2    Tan, I.3    Manser, E.4    Lim, L.5
  • 10
    • 0029786313 scopus 로고    scopus 로고
    • Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)
    • Amano, M. et al. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271, 20246-20249 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 20246-20249
    • Amano, M.1
  • 11
    • 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
  • 12
    • 0035877583 scopus 로고    scopus 로고
    • Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton
    • Tan, I., Ng, C. H., Lim, L. & Leung, T. Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton. J. Biol. Chem. 276, 21209-21216 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21209-21216
    • Tan, I.1    Ng, C.H.2    Lim, L.3    Leung, T.4
  • 13
    • 0022410257 scopus 로고
    • Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase
    • Ikebe, M. & Hartshorne, D. J. Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. J. Biol. Chem. 260, 10027-10031 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 10027-10031
    • Ikebe, M.1    Hartshorne, D.J.2
  • 14
    • 2142828492 scopus 로고    scopus 로고
    • ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts
    • Komatsu, S. & Ikebe, M. ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts. J. Cell Biol. 165, 243-254 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 243-254
    • Komatsu, S.1    Ikebe, M.2
  • 15
    • 0033615977 scopus 로고    scopus 로고
    • Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo
    • Kawano, Y. et al. Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J. Cell Biol. 147, 1023-1038 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1023-1038
    • Kawano, Y.1
  • 16
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng, J. et al. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274, 37385-37390 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37385-37390
    • Feng, J.1
  • 17
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation
    • Mills, J. C., Stone, N.L., Erhardt, J. & Pittman, R. N. Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J. Cell Biol. 140, 627-636 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 627-636
    • Mills, J.C.1    Stone, N.L.2    Erhardt, J.3    Pittman, R.N.4
  • 18
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor
    • Straight, A. F. et al. Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor. Science 299, 1743-1747 (2003).
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1
  • 19
    • 2142847315 scopus 로고    scopus 로고
    • Reconstructing leukocyte migration in 3D extracellular matrix by time-lapse videomicroscopy and computer-assisted tracking
    • Friedl, P. & Brocker, E. B. Reconstructing leukocyte migration in 3D extracellular matrix by time-lapse videomicroscopy and computer-assisted tracking. Methods Mol. Biol. 239, 77-90 (2004).
    • (2004) Methods Mol. Biol. , vol.239 , pp. 77-90
    • Friedl, P.1    Brocker, E.B.2
  • 20
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • Mukai, H. The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC. J. Biochem. (Tokyo) 133, 17-27 (2003).
    • (2003) J. Biochem. (Tokyo) , vol.133 , pp. 17-27
    • Mukai, H.1
  • 21
    • 0035079891 scopus 로고    scopus 로고
    • Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha
    • Tan, I., Seow, K. T., Lim, L. & Leung, T. Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha. Mol. Cell. Biol. 21, 2767-2778 (2001).
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2767-2778
    • Tan, I.1    Seow, K.T.2    Lim, L.3    Leung, T.4
  • 22
    • 0033853336 scopus 로고    scopus 로고
    • Phosphorylation of ERM proteins at filopodia induced by Cdc42
    • Nakamura, N. et al. Phosphorylation of ERM proteins at filopodia induced by Cdc42. Genes Cells 5, 571-581 (2000).
    • (2000) Genes Cells , vol.5 , pp. 571-581
    • Nakamura, N.1
  • 23
    • 0036011166 scopus 로고    scopus 로고
    • Cdc42 antagonizes inductive action of cAMP on cell shape, via effects of the myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) on myosin light chain phosphorylation
    • Dong, J. M., Leung, T., Manser, E. & Lim, L. Cdc42 antagonizes inductive action of cAMP on cell shape, via effects of the myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) on myosin light chain phosphorylation. Eur. J. Cell Biol. 81, 231-242 (2002).
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 231-242
    • Dong, J.M.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 24
    • 0029976102 scopus 로고    scopus 로고
    • Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity
    • Ichikawa, K., Ito, M. & Hartshorne, D. J. Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity. J. Biol. Chem. 271, 4733-4740 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 4733-4740
    • Ichikawa, K.1    Ito, M.2    Hartshorne, D.J.3
  • 26
    • 0033577902 scopus 로고    scopus 로고
    • p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts
    • Sells, M. A., Boyd, J. T. & Chernoff, J. p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts. J. Cell Biol. 145, 837-849 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 837-849
    • Sells, M.A.1    Boyd, J.T.2    Chernoff, J.3
  • 27
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders, L. C., Matsumura, F., Bokoch, G. M. & de Lanerolle, P. Inhibition of myosin light chain kinase by p21-activated kinase. Science 283, 2083-2085 (1999).
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    de Lanerolle, P.4
  • 28
    • 5444248307 scopus 로고    scopus 로고
    • Tenascin-C and SF/HGF produced by myofibroblasts in vitro provide convergent pro-invasive signals to human colon cancer cells through RhoA and Rac
    • De Wever, O. et al. Tenascin-C and SF/HGF produced by myofibroblasts in vitro provide convergent pro-invasive signals to human colon cancer cells through RhoA and Rac. FASEB J. 18, 1016-1018 (2004).
    • (2004) FASEB J. , vol.18 , pp. 1016-1018
    • De Wever, O.1
  • 29
    • 0032935495 scopus 로고    scopus 로고
    • An essential part for Rho-associated kinase in the transcellular invasion of tumor cells
    • Itoh, K. et al. An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nature Med. 5, 221-225 (1999).
    • (1999) Nature Med. , vol.5 , pp. 221-225
    • Itoh, K.1
  • 30
    • 0032539001 scopus 로고    scopus 로고
    • The transcription factor AP-1 is required for EGF-induced activation of rho-like GTPases, cytoskeletal rearrangements, motility, and in vitro invasion of A431 cells
    • Malliri, A. et al. The transcription factor AP-1 is required for EGF-induced activation of rho-like GTPases, cytoskeletal rearrangements, motility, and in vitro invasion of A431 cells. J. Cell Biol. 143, 1087-1099 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1087-1099
    • Malliri, A.1


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