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Volumn 308, Issue 2, 2005, Pages 422-438

Role of Rho, Rac, and Rho-kinase in phosphorylation of myosin light chain, development of polarity, and spontaneous migration of Walker 256 carcinosarcoma cells

Author keywords

Cell migration; Membrane blebbing; Myosin light chain; Myosin light chain kinase; Rac; Rho; Rho kinase; Walker carcinosarcoma cell

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; BLEBBISTATIN; EXOENZYME C3; MUTANT PROTEIN; MYOSIN; RAC PROTEIN; RHO KINASE; STATIN; UNCLASSIFIED DRUG; ENZYME INHIBITOR; MYOSIN II; MYOSIN LIGHT CHAIN; PROTEIN SERINE THREONINE KINASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHO-ASSOCIATED KINASE; RND1 PROTEIN, HUMAN; SIGNAL PEPTIDE;

EID: 24944513184     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.05.001     Document Type: Article
Times cited : (54)

References (45)
  • 1
    • 0345059766 scopus 로고    scopus 로고
    • Intravital imaging of cell movement in tumours
    • J. Condeelis, and J.E. Segall Intravital imaging of cell movement in tumours Nat. Rev., Cancer 3 2003 921 930
    • (2003) Nat. Rev., Cancer , vol.3 , pp. 921-930
    • Condeelis, J.1    Segall, J.E.2
  • 3
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • G.M. Bokoch, B.P. Bohl, and T.H. Chuang Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins J. Biol. Chem. 269 1994 31674 31679
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 4
    • 0034308228 scopus 로고    scopus 로고
    • Rho family GTPases: More than simple switches
    • M. Symons, and J. Settleman Rho family GTPases: more than simple switches Trends Cell Biol. 10 2000 415 419
    • (2000) Trends Cell Biol. , vol.10 , pp. 415-419
    • Symons, M.1    Settleman, J.2
  • 5
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • S. Etienne-Manneville, and A. Hall Rho GTPases in cell biology Nature 420 2002 629 635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 6
    • 6344231714 scopus 로고    scopus 로고
    • Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility
    • A.P. Wheeler, and A.J. Ridley Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility Exp. Cell Res. 301 2004 43 49
    • (2004) Exp. Cell Res. , vol.301 , pp. 43-49
    • Wheeler, A.P.1    Ridley, A.J.2
  • 8
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • O. Nakagawa, K. Fujisawa, T. Ishizaki, Y. Saito, K. Nakao, and S. Narumiya ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice FEBS Lett. 392 1996 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
  • 10
    • 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
    • T. Leung, X.Q. Chen, E. Manser, and L. Lim 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 1996 5313 5327
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 11
    • 0032496146 scopus 로고    scopus 로고
    • Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis
    • H. Goto, H. Kosako, K. Tanabe, M. Yanagida, M. Sakurai, M. Amano, K. Kaibuchi, and M. Inagaki Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis J. Biol. Chem. 273 1998 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
  • 14
    • 0032991828 scopus 로고    scopus 로고
    • Rho-kinase in human neutrophils: A role in signalling for myosin light chain phosphorylation and cell migration
    • V. Niggli Rho-kinase in human neutrophils: a role in signalling for myosin light chain phosphorylation and cell migration FEBS Lett. 445 1999 69 72
    • (1999) FEBS Lett. , vol.445 , pp. 69-72
    • Niggli, V.1
  • 16
    • 0030111475 scopus 로고    scopus 로고
    • Myosin II function in non-muscle cells
    • S.K. Maciver Myosin II function in non-muscle cells BioEssays 18 1996 179 182
    • (1996) BioEssays , vol.18 , pp. 179-182
    • MacIver, S.K.1
  • 17
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • D.J. Hartshorne, M. Ito, and F. Erdodi Myosin light chain phosphatase: subunit composition, interactions and regulation J. Muscle Res. Cell Motil. 19 1998 325 341
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 18
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • K.E. Kamm, and J.T. Stull Dedicated myosin light chain kinases with diverse cellular functions J. Biol. Chem. 276 2001 4527 4530
    • (2001) J. Biol. Chem. , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 19
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and non-muscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and non-muscle myosin II: modulated by G proteins, kinases, and myosin phosphatase Physiol. Rev. 83 2003 1325 1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 20
    • 0842288222 scopus 로고    scopus 로고
    • Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
    • G. Totsukawa, Y. Wu, Y. Sasaki, D.J. Hartshorne, Y. Yamakita, S. Yamashiro, and F. Matsumara Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts J. Cell Biol. 164 2004 427 439
    • (2004) J. Cell Biol. , vol.164 , pp. 427-439
    • Totsukawa, G.1    Wu, Y.2    Sasaki, Y.3    Hartshorne, D.J.4    Yamakita, Y.5    Yamashiro, S.6    Matsumara, F.7
  • 21
    • 0029870635 scopus 로고    scopus 로고
    • Protrusive activity quantitatively determines the rate and direction of cell locomotion
    • H.U. Keller, and H. Bebie Protrusive activity quantitatively determines the rate and direction of cell locomotion Cell Motil. Cytoskeleton 33 1996 241 251
    • (1996) Cell Motil. Cytoskeleton , vol.33 , pp. 241-251
    • Keller, H.U.1    Bebie, H.2
  • 22
    • 0036227092 scopus 로고    scopus 로고
    • Phenotype modulation in non-adherent and adherent sublines of Walker carcinosarcoma cells: The role of cell-substratum contacts and microtubules in controlling cell shape, locomotion and cytoskeletal structure
    • J. Sroka, M. von Gunten, G.A. Dunn, and H.U. Keller Phenotype modulation in non-adherent and adherent sublines of Walker carcinosarcoma cells: the role of cell-substratum contacts and microtubules in controlling cell shape, locomotion and cytoskeletal structure Int. J. Biochem. Cell Biol. 34 2002 882 899
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 882-899
    • Sroka, J.1    Von Gunten, M.2    Dunn, G.A.3    Keller, H.U.4
  • 23
    • 0035869651 scopus 로고    scopus 로고
    • The Rho/Rho-kinase and the phosphatidylinositol 3-kinase pathway are essential for spontaneous locomotion of Walker 256 carcinosarcoma cells
    • A. Wicki, and V. Niggli The Rho/Rho-kinase and the phosphatidylinositol 3-kinase pathway are essential for spontaneous locomotion of Walker 256 carcinosarcoma cells Int. J. Cancer 91 2001 763 771
    • (2001) Int. J. Cancer , vol.91 , pp. 763-771
    • Wicki, A.1    Niggli, V.2
  • 24
    • 0031454951 scopus 로고    scopus 로고
    • Integrin-dependent translocation of p160ROCK to cytoskeletal complex in thrombin-stimulated human platelets
    • A. Fujita, Y. Saito, T. Ishizaki, M. Maekawa, K. Fujisawa, and F. Ushikubi Integrin-dependent translocation of p160ROCK to cytoskeletal complex in thrombin-stimulated human platelets Biochem. J. 328 1997 769 775
    • (1997) Biochem. J. , vol.328 , pp. 769-775
    • Fujita, A.1    Saito, Y.2    Ishizaki, T.3    Maekawa, M.4    Fujisawa, K.5    Ushikubi, F.6
  • 25
    • 0029087973 scopus 로고
    • Nuclear delivery of antisense oligodeoxynucleotides through reversible permeabilization of human leukemia cells with streptolysin O
    • D.G. Spiller, and D.M. Tidd Nuclear delivery of antisense oligodeoxynucleotides through reversible permeabilization of human leukemia cells with streptolysin O Antisense Res. Dev. 5 1995 13 21
    • (1995) Antisense Res. Dev. , vol.5 , pp. 13-21
    • Spiller, D.G.1    Tidd, D.M.2
  • 26
    • 0031904453 scopus 로고    scopus 로고
    • Actin accumulation in pseudopods or in the tail of polarized Walker carcinosarcoma cells quantitatively correlates with local folding of the cell surface membrane
    • H.U. Keller, and P. Eggli Actin accumulation in pseudopods or in the tail of polarized Walker carcinosarcoma cells quantitatively correlates with local folding of the cell surface membrane Cell Motil. Cytoskeleton 40 1998 342 353
    • (1998) Cell Motil. Cytoskeleton , vol.40 , pp. 342-353
    • Keller, H.U.1    Eggli, P.2
  • 27
    • 0033818298 scopus 로고    scopus 로고
    • Redundancy of lamellipodia in locomoting Walker carcinosarcoma cells
    • H.U. Keller Redundancy of lamellipodia in locomoting Walker carcinosarcoma cells Cell Motil. Cytoskeleton 46 2000 247 256
    • (2000) Cell Motil. Cytoskeleton , vol.46 , pp. 247-256
    • Keller, H.U.1
  • 28
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • A.J. Ridley, H.F. Paterson, C.L. Johnston, D. Diekmann, and A. Hall The small GTP-binding protein rac regulates growth factor-induced membrane ruffling Cell 70 1992 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
  • 29
    • 0030615004 scopus 로고    scopus 로고
    • P160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • T. Ishizaki, M. Naito, K. Fujisawa, N. Watanabe, Y. Saito, and S. Narumiya p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions FEBS Lett. 404 1997 118 124
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Watanabe, N.4    Saito, Y.5    Narumiya, S.6
  • 30
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • J. Bain, H. McLauchlan, M. Elliot, and P. Cohen The specificities of protein kinase inhibitors: an update Biochem. J. 371 2003 199 204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliot, M.3    Cohen, P.4
  • 33
    • 0035075597 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage induces MLC phosphorylation and apoptotic membrane blebbing
    • M. Sebbagh, C. Renvoize, J. Hamelin, N. Riche, J. Bertoglio, and J. Breard Caspase-3-mediated cleavage induces MLC phosphorylation and apoptotic membrane blebbing Nat. Cell Biol. 3 2001 346 352
    • (2001) Nat. Cell Biol. , vol.3 , pp. 346-352
    • Sebbagh, M.1    Renvoize, C.2    Hamelin, J.3    Riche, N.4    Bertoglio, J.5    Breard, J.6
  • 34
    • 4644225973 scopus 로고    scopus 로고
    • Regulation of myosin light chain phosphorylation by RhoB in neuronal cells
    • A.M. Conway, A.B. James, E. O'Kane, S. Rakhit, and B.J. Morris Regulation of myosin light chain phosphorylation by RhoB in neuronal cells Exp. Cell Res. 300 2004 35 42
    • (2004) Exp. Cell Res. , vol.300 , pp. 35-42
    • Conway, A.M.1    James, A.B.2    O'Kane, E.3    Rakhit, S.4    Morris, B.J.5
  • 36
    • 0142124454 scopus 로고    scopus 로고
    • Signaling to migration in neutrophils: Importance of localized pathways
    • V. Niggli Signaling to migration in neutrophils: importance of localized pathways Int. J. Biochem. Cell Biol. 35 2003 1619 1638
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 1619-1638
    • Niggli, V.1
  • 37
    • 0032700438 scopus 로고    scopus 로고
    • Rho GTPases control migration and polarization of adhesion molecules and cytoskeletal ERM components in T lymphocytes
    • M.A. del Pozo, M. Vicente-Manzanares, R. Tejedor, J.M. Serrador, and F. Sanchez-Madrid Rho GTPases control migration and polarization of adhesion molecules and cytoskeletal ERM components in T lymphocytes Eur. J. Immunol. 29 1999 3609 3620
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3609-3620
    • Del Pozo, M.A.1    Vicente-Manzanares, M.2    Tejedor, R.3    Serrador, J.M.4    Sanchez-Madrid, F.5
  • 38
    • 18044386967 scopus 로고    scopus 로고
    • The role of RhoA in the regulation of cell morphology and motility
    • V. Tkach, E. Bock, and V. Berezin The role of RhoA in the regulation of cell morphology and motility Cell Motil. Cytoskeleton. 61 2005 21 33
    • (2005) Cell Motil. Cytoskeleton. , vol.61 , pp. 21-33
    • Tkach, V.1    Bock, E.2    Berezin, V.3
  • 39
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • D.C. Edwards, L.C. Sanders, G.M. Bokoch, and G.N. Gill Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics Nat. Cell Biol. 1 1999 253 259
    • (1999) Nat. Cell Biol. , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 40
    • 3042847368 scopus 로고    scopus 로고
    • Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells
    • H. Brzeska, J. Szczepanowska, F. Matsumura, and E.D. Korn Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells Cell Motil. Cytoskeleton 58 2004 186 199
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 186-199
    • Brzeska, H.1    Szczepanowska, J.2    Matsumura, F.3    Korn, E.D.4
  • 43
    • 0344012487 scopus 로고    scopus 로고
    • Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction
    • J. Kolega Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction Mol. Biol. Cell 14 2003 4745 4757
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4745-4757
    • Kolega, J.1
  • 45
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I
    • M.L. Coleman, E.A. Sahai, M. Yeo, M. Bosch, A. Dewar, and M.F. Olson Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I Nat. Cell Biol. 3 2001 339 345
    • (2001) Nat. Cell Biol. , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dewar, A.5    Olson, M.F.6


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