메뉴 건너뛰기




Volumn 9, Issue 12, 1999, Pages 640-648

Interplay between Rac and Rho in the control of substrate contact dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL INTERACTION; CELL MOTION; CYTOSKELETON; GUANOSINE TRIPHOSPHATASE; MYOSIN; SIGNAL TRANSDUCTION;

EID: 0033577975     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80286-3     Document Type: Article
Times cited : (528)

References (42)
  • 1
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder SM, Burridge K: Bidirectional signaling between the cytoskeleton and integrins. Curr Opin Cell Biol 1999, 11274-286.
    • (1999) Curr Opin Cell Biol , pp. 11274-11286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 3
    • 0027875911 scopus 로고
    • On the mechanisms of cortical actin flow and its role in cytoskeletal organisation of fibroblasts
    • Edited by Jones G, Wigley C, Warn R. The Company of Biologists Ltd
    • Heath JP, Holifield BF: On the mechanisms of cortical actin flow and its role in cytoskeletal organisation of fibroblasts. In Cell Behaviour: Adhesion and Motility. Edited by Jones G, Wigley C, Warn R. The Company of Biologists Ltd; 1993:35-56.
    • (1993) Cell Behaviour: Adhesion and Motility , pp. 35-56
    • Heath, J.P.1    Holifield, B.F.2
  • 4
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hal A: Rho GTPases and the actin cytoskeleton. Science 1998, 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hal, A.1
  • 5
    • 0002428359 scopus 로고
    • Cytostructural dynamics of contact formation during fibroblast locomotion in vitro
    • Small JV, Rinnerthaler G: Cytostructural dynamics of contact formation during fibroblast locomotion in vitro. Exp Biol Med 1985, 10:54-68.
    • (1985) Exp Biol Med , vol.10 , pp. 54-68
    • Small, J.V.1    Rinnerthaler, G.2
  • 6
    • 0023851499 scopus 로고
    • Contact formation during fibroblast locomotion: Involvement of membrane ruffles and microtubules
    • Rinnerthaler G, Geiger B, Small JV: Contact formation during fibroblast locomotion: Involvement of membrane ruffles and microtubules. J Cell Biol 1988, 106:747-760.
    • (1988) J Cell Biol , vol.106 , pp. 747-760
    • Rinnerthaler, G.1    Geiger, B.2    Small, J.V.3
  • 7
    • 0019230475 scopus 로고
    • Formation of cell to substrate contacts during fibroblast motility. An interference reflexion study
    • Izzard CS, Lochner LR: Formation of cell to substrate contacts during fibroblast motility. An interference reflexion study. J Cell Sci 1980, 42:81-116.
    • (1980) J Cell Sci , vol.42 , pp. 81-116
    • Izzard, C.S.1    Lochner, L.R.2
  • 8
    • 0020999298 scopus 로고
    • Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction
    • Burridge K, Connell L: Talin: a cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction. Cell Motil Cytoskel 1983, 3:405-417.
    • (1983) Cell Motil Cytoskel , vol.3 , pp. 405-417
    • Burridge, K.1    Connell, L.2
  • 9
    • 0023567964 scopus 로고
    • Evidence for an actin-containing cytoplasmic precursor of the focal contact and the timing of incorporation of vinculin at the focal contact
    • DePasquale JA, Izzard CS: Evidence for an actin-containing cytoplasmic precursor of the focal contact and the timing of incorporation of vinculin at the focal contact. J Cell Biol 1987, 105:2803-2809.
    • (1987) J Cell Biol , vol.105 , pp. 2803-2809
    • DePasquale, J.A.1    Izzard, C.S.2
  • 10
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A: Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 11
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the Rho family of GTPases
    • Clark EA, King WG, Bugge JS, Symons M, Hynes RO: Integrin-mediated signals regulated by members of the Rho family of GTPases. J Cell Biol 1998, 142:573-586.
    • (1998) J Cell Biol , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Bugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 12
    • 0030940218 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages
    • Allen WE, Jones GE, Pollard JW, Ridley AJ: Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages. J Cell Sci 1997, 110:707-720.
    • (1997) J Cell Sci , vol.110 , pp. 707-720
    • Allen, W.E.1    Jones, G.E.2    Pollard, J.W.3    Ridley, A.J.4
  • 13
    • 0027435176 scopus 로고
    • Localization and dynamics of nonfilamentous actin in cultured cells
    • Cao LG, Fishkind DJ, Wang YL: Localization and dynamics of nonfilamentous actin in cultured cells. J Cell Biol 1993, 123:173-181.
    • (1993) J Cell Biol , vol.123 , pp. 173-181
    • Cao, L.G.1    Fishkind, D.J.2    Wang, Y.L.3
  • 16
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka M, Burridge K: Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 1996, 133:1403-1415.
    • (1996) J Cell Biol , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 17
    • 0026409760 scopus 로고
    • Myosin-light-chain kinase inhibitors ML-7 and ML-9 inhibit mouse lung carcinoma cell attachment to the fibronectin substratum
    • Isemura M, Mita T, Satoh K, Narumi K, Motomiya M: Myosin-light-chain kinase inhibitors ML-7 and ML-9 inhibit mouse lung carcinoma cell attachment to the fibronectin substratum. Cell Biol Int Rep 1991, 15:965-972.
    • (1991) Cell Biol Int Rep , vol.15 , pp. 965-972
    • Isemura, M.1    Mita, T.2    Satoh, K.3    Narumi, K.4    Motomiya, M.5
  • 19
    • 0029098971 scopus 로고
    • Myosin is involved in postmitotic cell spreading
    • Cramer LP, Mitchison TJ: Myosin is involved in postmitotic cell spreading. J Cell Biol 1995, 131:179-189.
    • (1995) J Cell Biol , vol.131 , pp. 179-189
    • Cramer, L.P.1    Mitchison, T.J.2
  • 20
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/ rac GTPases
    • Hotchin NA, Hall A: The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/ rac GTPases. J Cell Biol 1995, 131:1857-1865.
    • (1995) J Cell Biol , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 21
    • 0033134836 scopus 로고    scopus 로고
    • 2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments
    • 2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments. J Physiol 1999, 516:805-824.
    • (1999) J Physiol , vol.516 , pp. 805-824
    • Weber, L.P.1    Van Lierop, J.E.2    Walsh, M.P.3
  • 22
    • 0026706241 scopus 로고
    • Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum
    • Just I, Mohr C, Schallehn G, Menard L, Didsbury JR, Vandekerckhove J, et al.: Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum. J Biol Chem 1992, 267:10274-10280.
    • (1992) J Biol Chem , vol.267 , pp. 10274-10280
    • Just, I.1    Mohr, C.2    Schallehn, G.3    Menard, L.4    Didsbury, J.R.5    Vandekerckhove, J.6
  • 25
    • 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 C, Van Aelst L: Rac regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science 1996, 22:1374-1376.
    • (1996) Science , vol.22 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar-Sagi, C.3    Van Aelst, L.4
  • 26
    • 0031027205 scopus 로고    scopus 로고
    • Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
    • Kozma R, Sarner S, Ahmed S, Lim L: Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol Cell Biol 1997, 17:1201-1211.
    • (1997) Mol Cell Biol , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 27
    • 0030658939 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor Tiam 1 affects neuronal morphology; opposing roles for the small GTPases Rac and Rho
    • Van Leeuwen FN, Kain HET, Van der Kammen RA, Michiels F, Kranenburg OW, Collard JG: The guanine nucleotide exchange factor Tiam 1 affects neuronal morphology; opposing roles for the small GTPases Rac and Rho. J Cell Biol 1997, 139:797-807.
    • (1997) J Cell Biol , vol.139 , pp. 797-807
    • Van Leeuwen, F.N.1    Kain, H.E.T.2    Van Der Kammen, R.A.3    Michiels, F.4    Kranenburg, O.W.5    Collard, J.G.6
  • 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, Ishizaki T, Watanabe N, Uehata M, Kranenburg O, Moolenaar WH, et al.: Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 Cells. J Cell Biol 1998, 41:1625-1636.
    • (1998) J Cell Biol , vol.41 , pp. 1625-1636
    • Hirose, M.1    Ishizaki, T.2    Watanabe, N.3    Uehata, M.4    Kranenburg, O.5    Moolenaar, W.H.6
  • 30
    • 0024425742 scopus 로고
    • Talin dynamics in living microinjected nonmuscle cells
    • Hock RS, Sanger JM, Sanger JW: Talin dynamics in living microinjected nonmuscle cells. Cell Motil Cytoskel 1989, 14:271-287.
    • (1989) Cell Motil Cytoskel , vol.14 , pp. 271-287
    • Hock, R.S.1    Sanger, J.M.2    Sanger, J.W.3
  • 31
    • 0020417653 scopus 로고
    • Microinjection of fluorescently labeled proteins into living cells with emphasis on cytoskeletal proteins
    • Kreis TE, Birchmeier W : Microinjection of fluorescently labeled proteins into living cells with emphasis on cytoskeletal proteins. Int Rev Cytol 1982, 75:209-227.
    • (1982) Int Rev Cytol , vol.75 , pp. 209-227
    • Kreis, T.E.1    Birchmeier, W.2
  • 33
    • 0013618357 scopus 로고
    • Analysis of cytoskeletal structures by the microinjection of fluorescent probes
    • Wiley-Liss nc
    • Wang YL, Sanders MC: Analysis of cytoskeletal structures by the microinjection of fluorescent probes. In Noninvasive Tech Cell Biol Wiley-Liss nc; 1990:177-212.
    • (1990) Noninvasive Tech Cell Biol , pp. 177-212
    • Wang, Y.L.1    Sanders, M.C.2
  • 34
    • 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 1997, 410:68-72.
    • (1997) FEBS Lett , vol.410 , pp. 68-72
    • Narumiya, S.1    Ishizaki, T.2    Watanabe, N.3
  • 35
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
    • Uehata M, Ishizaki T, Satoh H, Ono T, Kawahara T, Morishita H, et al.: Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature 1997, 389:990-994.
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1    Ishizaki, T.2    Satoh, H.3    Ono, T.4    Kawahara, T.5    Morishita, H.6
  • 36
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C, Chrzanowska-Wodnicka M, Brown J, Shaub A, Belkin AM, Burridge K: Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J Cell Biol 1998, 141:539-551.
    • (1998) J Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 37
    • 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, Madaule P, Reid T, Ishizaki T, Watanabe G, Kakizuka A, 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 1997, 16:3044-3056.
    • (1997) EMBO J , vol.16 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6
  • 38
    • 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 AJ, Hall A: The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors, Cell 1992,70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 39
    • 0033531237 scopus 로고    scopus 로고
    • A balance of signaling by Rho family small GTpases RhoA, Rac1 and Cdc42 coordinates cytoskeletal morphology but not cell survival
    • Moorman JP, Luu D, Wickham J, Bobak DA, Hahn CS: A balance of signaling by Rho family small GTpases RhoA, Rac1 and Cdc42 coordinates cytoskeletal morphology but not cell survival. Oncogens 1999, 18:47-57.
    • (1999) Oncogens , vol.18 , pp. 47-57
    • Moorman, J.P.1    Luu, D.2    Wickham, J.3    Bobak, D.A.4    Hahn, C.S.5
  • 40
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes
    • Manser E, Huang HY, Loo TH, Chen XQ, Dong JM, Leung T, et al.: Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes. Mol Cell Biol 1997, 17:1129-1143.
    • (1997) Mol Cell Biol , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6
  • 41
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin-light-chain-kinase by p21-activated kinase
    • Sanders LC, Matsumura F, Bokoch GM, de Lanerolle P: Inhibition of myosin-light-chain-kinase by p21-activated kinase. Science 1999, 283:2083-2085.
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    De Lanerolle, P.4
  • 42
    • 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, et al.: p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett 1997, 10:118-124.
    • (1997) FEBS Lett , vol.10 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.