메뉴 건너뛰기




Volumn 16, Issue 1, 2005, Pages 84-96

R-Ras controls membrane protrusion and cell migration through the spatial regulation of Rac and Rho

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN; R RAS PROTEIN; RAC PROTEIN; RAS PROTEIN; RHO FACTOR; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 11144322264     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-04-0277     Document Type: Article
Times cited : (78)

References (69)
  • 1
    • 0035157971 scopus 로고    scopus 로고
    • Activation of Rhoa and ROCK are essential for detachment of migrating leukocytes
    • Alblas, J., Ulfman, L., Hordijk, P., and Koenderman, L. (2001). Activation of Rhoa and ROCK are essential for detachment of migrating leukocytes. Mol. Biol. Cell 12, 2137-2145.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2137-2145
    • Alblas, J.1    Ulfman, L.2    Hordijk, P.3    Koenderman, L.4
  • 2
    • 0032100809 scopus 로고    scopus 로고
    • A role for Cdc42 in macrophage chemotaxis
    • Allen, W. E., Zicha, D., Ridley, A. J., and Jones, G. E. (1998). A role for Cdc42 in macrophage chemotaxis. J. Cell Biol. 141, 1147-1157.
    • (1998) J. Cell Biol. , vol.141 , pp. 1147-1157
    • Allen, W.E.1    Zicha, D.2    Ridley, A.J.3    Jones, G.E.4
  • 3
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppressed RhoA activity via a c-Src-dependent mechanism
    • Arthur, W. T., Petch, L. A., and Burridge, K. (2000). Integrin engagement suppressed RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10, 719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 4
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • Arthur, W. T., and Burridge, K. (2001). RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell 12, 2711-2720.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 5
    • 0034719380 scopus 로고    scopus 로고
    • Motility and invasion are differentially modulated by Rho family GTPases
    • Banyard, J., Anand-Apte, B., Symons, M., and Zetter, B. R. (2000). Motility and invasion are differentially modulated by Rho family GTPases. Oncogene 19, 580-591.
    • (2000) Oncogene , vol.19 , pp. 580-591
    • Banyard, J.1    Anand-Apte, B.2    Symons, M.3    Zetter, B.R.4
  • 6
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
    • Bear, J. E. et al. (2002). Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell. 109, 509-521.
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1
  • 7
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo, K. A., Dembo, M., Kaverina, I., Small, J. V., and Wang, Y. L. (2001). Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153, 881-888.
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 8
    • 3543072944 scopus 로고    scopus 로고
    • Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function
    • Berdeaux, R. L., Diaz, B., Kim, L., and Martin, G. S. (2004). Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function. J. Cell Biol. 166, 317-323.
    • (2004) J. Cell Biol. , vol.166 , pp. 317-323
    • Berdeaux, R.L.1    Diaz, B.2    Kim, L.3    Martin, G.S.4
  • 9
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A. L., and Hall, A. (2000). Rho GTPases and their effector proteins. Biochem. J. 348(Pt 2), 241-255.
    • (2000) Biochem. J. , vol.348 , Issue.PART 2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 10
    • 0038305915 scopus 로고    scopus 로고
    • ERK and RhoA differentially regulate pseudopodia growth and retraction during chemotaxis
    • Brahmbhatt, A. A., and Klemke, R. L. (2003). ERK and RhoA differentially regulate pseudopodia growth and retraction during chemotaxis. J. Biol. Chem. 278, 13016-13025.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13016-13025
    • Brahmbhatt, A.A.1    Klemke, R.L.2
  • 11
    • 0037474267 scopus 로고    scopus 로고
    • Oncogenic Ras leads to Rho activation by activating the mitogen-activated protein kinase pathway and decreasing Rho-GTPase-activating protein activity
    • Chen, J. C., Zhuang, S., Nguyen, T. H., Boss, G. R., and Pilz, R. B. (2003). Oncogenic Ras leads to Rho activation by activating the mitogen-activated protein kinase pathway and decreasing Rho-GTPase-activating protein activity. J. Biol. Chem. 278, 2807-2818.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2807-2818
    • Chen, J.C.1    Zhuang, S.2    Nguyen, T.H.3    Boss, G.R.4    Pilz, R.B.5
  • 12
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho, S. Y., and Klemke, R. L. (2002). Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J. Cell Biol. 156, 725-736.
    • (2002) J. Cell Biol. , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 13
    • 0035152391 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases
    • Cox, E. A., Sastry, S. K., and Huttenlocher, A. (2001). Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases. Mol. Biol. Cell 12, 265-277.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 265-277
    • Cox, E.A.1    Sastry, S.K.2    Huttenlocher, A.3
  • 14
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
    • del Pozo, M. A., Price, L. S., Alderson, N. B., Ren, X. D., and Schwartz, M. A. (2000). Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19, 2008-2014.
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • Del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.D.4    Schwartz, M.A.5
  • 15
    • 0042171820 scopus 로고    scopus 로고
    • Rho activation patterns after spinal cord injury and the role of activated Rho in apoptosis in the central nervous system
    • Dubreuil, C. I., Winton, M. J., and McKerracher, L. (2003). Rho activation patterns after spinal cord injury and the role of activated Rho in apoptosis in the central nervous system. J. Cell Biol. 162, 233-243.
    • (2003) J. Cell Biol. , vol.162 , pp. 233-243
    • Dubreuil, C.I.1    Winton, M.J.2    McKerracher, L.3
  • 16
    • 2342548182 scopus 로고    scopus 로고
    • p75 neurotrophin receptor signaling regulates growth cone filopodial dynamics through modulating RhoA activity
    • Gehler, S., Gallo, G., Veien, E., and Letourneau, P. C. (2004). p75 Neurotrophin receptor signaling regulates growth cone filopodial dynamics through modulating RhoA activity. J. Neurosci. 24(18):4363-4372.
    • (2004) J. Neurosci. , vol.24 , Issue.18 , pp. 4363-4372
    • Gehler, S.1    Gallo, G.2    Veien, E.3    Letourneau, P.C.4
  • 17
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and Ruoslahti, E. (1999). Integrin signaling. Science 285, 1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 18
    • 0033603826 scopus 로고    scopus 로고
    • Quantifying lamella dynamics of cultured cells by SACED, a new computer-assisted motion analysis
    • Hinz, B., Alt, W., Johnen, C., Herzog, V., and Kaiser, H. W. (1999). Quantifying lamella dynamics of cultured cells by SACED, a new computer-assisted motion analysis. Exp. Cell Res. 251, 234-243.
    • (1999) Exp. Cell Res. , vol.251 , pp. 234-243
    • Hinz, B.1    Alt, W.2    Johnen, C.3    Herzog, V.4    Kaiser, H.W.5
  • 19
    • 0033527623 scopus 로고    scopus 로고
    • Cell migration-movin'on
    • Horwitz, A. R., and Parsons, J. T. (1999). Cell migration-movin'on. Science 286, 1102-1103.
    • (1999) Science , vol.286 , pp. 1102-1103
    • Horwitz, A.R.1    Parsons, J.T.2
  • 20
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf-initiated MAP kinase pathway
    • Hughes, P. E., Renshaw, M. W., Pfaff, M., Forsyth, J., Keivens, V. M., Schwartz, M. A., and Ginsberg, M. H. (1997). Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway. Cell 88, 521-530.
    • (1997) Cell , vol.88 , pp. 521-530
    • Hughes, P.E.1    Renshaw, M.W.2    Pfaff, M.3    Forsyth, J.4    Keivens, V.M.5    Schwartz, M.A.6    Ginsberg, M.H.7
  • 21
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • Huttenlocher, A., Ginsberg, M. H., and Horwitz, A. F. (1996). Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J. Cell Biol. 134, 1551-1562.
    • (1996) J. Cell Biol. , vol.134 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 23
    • 0036773899 scopus 로고    scopus 로고
    • Temporal and spatial regulation of chemotaxis
    • Iijima, M., Huang, Y. I., and Devreotes, P. (2002). Temporal and spatial regulation of chemotaxis. Dev. Cell 3, 469-478.
    • (2002) Dev. Cell , vol.3 , pp. 469-478
    • Iijima, M.1    Huang, Y.I.2    Devreotes, P.3
  • 24
    • 0032481126 scopus 로고    scopus 로고
    • Possible involvement of the inactivation of the Rho-Rho-kinase pathway in oncogenic Ras-induced transformation
    • Izawa, I., Amano, M., Chihara, K., Yamamoto, T., and Kaibuchi, K. (1998). Possible involvement of the inactivation of the Rho-Rho-kinase pathway in oncogenic Ras-induced transformation. Oncogene 17, 2863-2871.
    • (1998) Oncogene , vol.17 , pp. 2863-2871
    • Izawa, I.1    Amano, M.2    Chihara, K.3    Yamamoto, T.4    Kaibuchi, K.5
  • 26
    • 0033620657 scopus 로고    scopus 로고
    • R-Ras signals through specific integrin alpha cytoplasmic domains to promote migration and invasion of breast epithelial cells
    • Keely, P. J., Rusyn, E. V., Cox, A. D., and Parise, L. V. (1999). R-Ras signals through specific integrin alpha cytoplasmic domains to promote migration and invasion of breast epithelial cells. J. Cell Biol. 145, 1077-1088.
    • (1999) J. Cell Biol. , vol.145 , pp. 1077-1088
    • Keely, P.J.1    Rusyn, E.V.2    Cox, A.D.3    Parise, L.V.4
  • 29
    • 0037304376 scopus 로고    scopus 로고
    • R-Ras promotes focal adhesion formation through focal adhesion kinase and p130(Cas) by a novel mechanism that differs from integrins
    • Kwong, L., Wozniak, M. A., Collins, A. S., Wilson, S. D., and Keely, P. J. (2003). R-Ras promotes focal adhesion formation through focal adhesion kinase and p130(Cas) by a novel mechanism that differs from integrins. Mol. Cell. Biol. 23, 933-949.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 933-949
    • Kwong, L.1    Wozniak, M.A.2    Collins, A.S.3    Wilson, S.D.4    Keely, P.J.5
  • 30
    • 0033621462 scopus 로고    scopus 로고
    • Potentiation of cell migration by adhesion-dependent cooperative signals from the GTPase Rac and Raf kinase
    • Leng, J., Klemke, R. L., Reddy, A. C., and Cheresh, D. A. (1999). Potentiation of cell migration by adhesion-dependent cooperative signals from the GTPase Rac and Raf kinase. J. Biol. Chem. 274, 37855-37861.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37855-37861
    • Leng, J.1    Klemke, R.L.2    Reddy, A.C.3    Cheresh, D.A.4
  • 31
    • 0037186083 scopus 로고    scopus 로고
    • Regulation of rho GTPases by crosstalk and neuronal activity in vivo
    • Li, Z., Aizenman, C. D., and Cline, H. T. (2002). Regulation of rho GTPases by crosstalk and neuronal activity in vivo. Neuron 33, 741-750.
    • (2002) Neuron , vol.33 , pp. 741-750
    • Li, Z.1    Aizenman, C.D.2    Cline, H.T.3
  • 32
    • 0023657439 scopus 로고
    • Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes
    • Lowe, D. G., Capon, D. J., Delwart, E., Sakaguchi, A. Y., Naylor, S. L., and Goeddel, D. V. (1987). Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes. Cell 48, 137-146.
    • (1987) Cell , vol.48 , pp. 137-146
    • Lowe, D.G.1    Capon, D.J.2    Delwart, E.3    Sakaguchi, A.Y.4    Naylor, S.L.5    Goeddel, D.V.6
  • 33
    • 0032400361 scopus 로고    scopus 로고
    • Deconstructing (and reconstructing) cell migration
    • Maheshwari, G., and Lauffenburger, D. A. (1998). Deconstructing (and reconstructing) cell migration. Microsc. Res. Tech. 43, 358-368.
    • (1998) Microsc. Res. Tech. , vol.43 , pp. 358-368
    • Maheshwari, G.1    Lauffenburger, D.A.2
  • 34
    • 0031038131 scopus 로고    scopus 로고
    • R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways
    • Marte, B. M., Rodriguez-Viciana, P., Wennstrom, S., Warne, P. H., and Downward, J. (1996). R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways. Curr. Biol. 7, 63-70.
    • (1996) Curr. Biol. , vol.7 , pp. 63-70
    • Marte, B.M.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 35
    • 0033117823 scopus 로고    scopus 로고
    • Structure and function of the Arp2/3 complex
    • Mullins, R. D., and Pollard, T. D. (1999). Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 9, 244-249.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 244-249
    • Mullins, R.D.1    Pollard, T.D.2
  • 36
    • 0035661651 scopus 로고    scopus 로고
    • Distinct roles of frontal and rear cell-substrate adhesions in fibroblast migration
    • Munevar, S., Wang, Y. L., and Dembo, M. (2001). Distinct roles of frontal and rear cell-substrate adhesions in fibroblast migration. Mol. Biol. Cell 12, 3947-3954.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3947-3954
    • Munevar, S.1    Wang, Y.L.2    Dembo, M.3
  • 37
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes, C. D., and Hall, A. (1999). Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144, 1235-1244.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 38
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek, S. P., Loftus, J. C., Ginsberg, M. H., Lauffenburger, D. A., and Horwitz, A. F. (1997). Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385, 537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 39
    • 0032475863 scopus 로고    scopus 로고
    • G protein signaling events are activated at the leading edge of chemotactic cells
    • Parent, C. A., Blacklock, B. J., Froehlich, W. M., Murphy, D. B., and Devreotes, P. N. (1998). G protein signaling events are activated at the leading edge of chemotactic cells. Cell 95, 81-91.
    • (1998) Cell , vol.95 , pp. 81-91
    • Parent, C.A.1    Blacklock, B.J.2    Froehlich, W.M.3    Murphy, D.B.4    Devreotes, P.N.5
  • 40
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou, M., and Hall, A. (2004). Cell migration: Rho GTPases lead the way. Dev. Biol. 265, 23-32.
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 41
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B., and Schwartz, M. A. (1999). Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 42
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley, A. J. (2001a). Rho family proteins: coordinating cell responses. Trends Cell Biol. 11, 471-477.
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 43
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley, A.J. (2001b). Rho GTPases and cell migration. J. Cell Sci. 114, 2713-2722.
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 45
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner, K., Hall, A., and Small, J. V. (1999). Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9, 640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 46
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander, E. E., ten Klooster, J.P., van Delft, S., van der Kammen, R. A., and Collard, J. G. (1999). Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147, 1009-1022.
    • (1999) J. Cell Biol. , vol.147 , pp. 1009-1022
    • Sander, E.E.1    Ten Klooster, J.P.2    Van Delft, S.3    Van Der Kammen, R.A.4    Collard, J.G.5
  • 47
    • 0031915021 scopus 로고    scopus 로고
    • Integrin signalling and tyrosine phosphorylation: Just the FAKs?
    • Schlaepfer, D. D., and Hunter, T. (1998). Integrin signalling and tyrosine phosphorylation: just the FAKs? Trends Cell Biol. 8, 151-157.
    • (1998) Trends Cell Biol. , vol.8 , pp. 151-157
    • Schlaepfer, D.D.1    Hunter, T.2
  • 48
    • 0035030515 scopus 로고    scopus 로고
    • Analysis of R-Ras signalling pathways
    • Self, A. J., Caron, E., Paterson, H. F., and Hall, A. (2001). Analysis of R-Ras signalling pathways. J. Cell Sci. 114, 1357-1366.
    • (2001) J. Cell Sci. , vol.114 , pp. 1357-1366
    • Self, A.J.1    Caron, E.2    Paterson, H.F.3    Hall, A.4
  • 49
    • 0032979447 scopus 로고    scopus 로고
    • The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway
    • Sethi, T., Ginsberg, M. H., Downward, J., and Hughes, P. E. (1999). The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway. Mol. Biol. Cell 10, 1799-1809.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1799-1809
    • Sethi, T.1    Ginsberg, M.H.2    Downward, J.3    Hughes, P.E.4
  • 51
    • 0031964022 scopus 로고    scopus 로고
    • Cell migration: Regulation of force on extracellular-matrix-integrin complexes
    • Sheetz, M. P., Felsenfeld, D. P., and Galbraith, C. G. (1998). Cell migration: regulation of force on extracellular-matrix-integrin complexes. Trends Cell Biol. 8, 51-54.
    • (1998) Trends Cell Biol. , vol.8 , pp. 51-54
    • Sheetz, M.P.1    Felsenfeld, D.P.2    Galbraith, C.G.3
  • 52
    • 0029870954 scopus 로고    scopus 로고
    • The war on cancer
    • Sporn, M. B. (1996). The war on cancer. Lancet 347, 1377-1381.
    • (1996) Lancet , vol.347 , pp. 1377-1381
    • Sporn, M.B.1
  • 54
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T. M., and Borisy, G. G. (1999). Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 55
    • 18444414614 scopus 로고    scopus 로고
    • ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts
    • Tsuji, T. et al. (2002). ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts. J. Cell Biol. 157, 819-830.
    • (2002) J. Cell Biol. , vol.157 , pp. 819-830
    • Tsuji, T.1
  • 56
    • 0036482512 scopus 로고    scopus 로고
    • Studying actin-dependent processes in tissue culture
    • Walpita, D., and Hay, E. (2002). Studying actin-dependent processes in tissue culture. Nat. Rev. Mol. Cell. Biol. 3, 137-141.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 137-141
    • Walpita, D.1    Hay, E.2
  • 57
    • 0035844149 scopus 로고    scopus 로고
    • Differential activation of the Rac pathway by Ha-Ras and K-Ras
    • Walsh, A. B., and Bar-Sagi, D. (2001). Differential activation of the Rac pathway by Ha-Ras and K-Ras. J. Biol. Chem. 276, 15609-15615.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15609-15615
    • Walsh, A.B.1    Bar-Sagi, D.2
  • 58
    • 0036308458 scopus 로고    scopus 로고
    • Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils
    • Wang, F., Herzmark, P., Weiner, O. D., Srinivasan, S., Servant, G., and Bourne, H. R. (2002). Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils. Nat. Cell Biol. 4, 513-518.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 513-518
    • Wang, F.1    Herzmark, P.2    Weiner, O.D.3    Srinivasan, S.4    Servant, G.5    Bourne, H.R.6
  • 59
    • 0344758986 scopus 로고    scopus 로고
    • Regulation of cell polarity and protrusion formation by targeting RhoA for degradation
    • Wang, H. R., Zhang, Y., Ozdamar, B., Ogunjimi, A. A., Alexandrova, E., Thomsen, G. H., and Wrana, J. L. (2003). Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302, 1775-1779.
    • (2003) Science , vol.302 , pp. 1775-1779
    • Wang, H.R.1    Zhang, Y.2    Ozdamar, B.3    Ogunjimi, A.A.4    Alexandrova, E.5    Thomsen, G.H.6    Wrana, J.L.7
  • 60
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells-over and over and over again
    • Webb, D. J., Parsons, J. T., and Horwitz, A. F. (2002). Adhesion assembly, disassembly and turnover in migrating cells-over and over and over again. Nat. Cell Biol. 4, E97-E100.
    • (2002) Nat. Cell Biol. , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 62
    • 0033231935 scopus 로고    scopus 로고
    • The world according to Arp: Regulation of actin nucleation by the Arp2/3 complex
    • Welch, M.D. (1999). The world according to Arp: regulation of actin nucleation by the Arp2/3 complex. Trends Cell Biol. 9, 423-427.
    • (1999) Trends Cell Biol. , vol.9 , pp. 423-427
    • Welch, M.D.1
  • 64
    • 0038037737 scopus 로고    scopus 로고
    • RhoA and ROCK promote migration by limiting membrane protrusions
    • Worthylake, R. A., and Burridge, K. (2003). RhoA and ROCK promote migration by limiting membrane protrusions. J. Biol. Chem. 278, 13578-13584.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13578-13584
    • Worthylake, R.A.1    Burridge, K.2
  • 65
    • 0035833247 scopus 로고    scopus 로고
    • RhoA is required for monocyte tail retraction during transendothelial migration
    • Worthylake, R. A., Lemoine, S., Watson, J. M., and Burridge, K. (2001). RhoA is required for monocyte tail retraction during transendothelial migration. J. Cell Biol. 154, 147-160.
    • (2001) J. Cell Biol. , vol.154 , pp. 147-160
    • Worthylake, R.A.1    Lemoine, S.2    Watson, J.M.3    Burridge, K.4
  • 66
    • 0242509224 scopus 로고    scopus 로고
    • ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix
    • Wozniak, M. A., Desai, R., Solski, P. A., Der, C. J., and Keely, P. J. (2003). ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix. J. Cell Biol. 163, 583-595.
    • (2003) J. Cell Biol. , vol.163 , pp. 583-595
    • Wozniak, M.A.1    Desai, R.2    Solski, P.A.3    Der, C.J.4    Keely, P.J.5
  • 68
    • 0035668525 scopus 로고    scopus 로고
    • Dbl family guanine nucleotide exchange factors
    • Zheng, Y. (2001). Dbl family guanine nucleotide exchange factors. Trends Biochem. Sci. 26, 724-732.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 724-732
    • Zheng, Y.1
  • 69
    • 0034658674 scopus 로고    scopus 로고
    • Oncogenic Ras down-regulates Rac activity, which leads to increased Rho activity and epithelial-mesenchymal transition
    • Zondag, G. C., Evers, E. E., ten Klooster, J. P., Janssen, L., van der Kammen, R. A., and Collard, J. G. (2000). Oncogenic Ras down-regulates Rac activity, which leads to increased Rho activity and epithelial-mesenchymal transition. J. Cell Biol. 149, 775-782.
    • (2000) J. Cell Biol. , vol.149 , pp. 775-782
    • Zondag, G.C.1    Evers, E.E.2    Ten Klooster, J.P.3    Janssen, L.4    Van Der Kammen, R.A.5    Collard, J.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.