메뉴 건너뛰기




Volumn 116, Issue 12, 2003, Pages 2389-2397

Coupling membrane protrusion and cell adhesion

Author keywords

Actin polymerization; Adhesion; Phagocytosis; Protrusion

Indexed keywords

CADHERIN; CELL PROTEIN; GUANOSINE TRIPHOSPHATASE; RHO FACTOR; VINCULIN;

EID: 0037484137     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00605     Document Type: Review
Times cited : (158)

References (116)
  • 1
    • 0014130852 scopus 로고
    • Contact inhibition: The phenomenon and its biological implications
    • Abercrombie, M. (1967). Contact inhibition: the phenomenon and its biological implications. Natl. Cancer Inst. Monogr. 26, 249-277.
    • (1967) Natl. Cancer Inst. Monogr. , vol.26 , pp. 249-277
    • Abercrombie, M.1
  • 2
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • Aderem, A. and Underhill, D. M. (1999). Mechanisms of phagocytosis in macrophages. Annu. Rev. Immunol. 17, 593-623.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 3
    • 0035159257 scopus 로고    scopus 로고
    • Efficient uptake of Yersinia pseudotuberculosis via integrin receptors involves a Rac1-Arp 2/3 pathway that bypasses N-WASP function
    • Alrutz, M. A., Srivastava, A., Wong, K. W., D'Souza-Schorey, C., Tang, M., Ch'Ng, L. E., Snapper, S. B. and Isberg, R. R. (2001). Efficient uptake of Yersinia pseudotuberculosis via integrin receptors involves a Rac1-Arp 2/3 pathway that bypasses N-WASP function. Mol. Microbiol. 42, 689-703.
    • (2001) Mol. Microbiol. , vol.42 , pp. 689-703
    • Alrutz, M.A.1    Srivastava, A.2    Wong, K.W.3    D'Souza-Schorey, C.4    Tang, M.5    Ch'Ng, L.E.6    Snapper, S.B.7    Isberg, R.R.8
  • 4
    • 0345593816 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts
    • Angers-Loustau, A., Cote, J. F., Charest, A., Dowbenko, D., Spencer, S., Lasky, L. A. and Tremblay, M. L. (1999). Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts. J. Cell Biol. 144, 1019-1031.
    • (1999) J. Cell Biol. , vol.144 , pp. 1019-1031
    • Angers-Loustau, A.1    Cote, J.F.2    Charest, A.3    Dowbenko, D.4    Spencer, S.5    Lasky, L.A.6    Tremblay, M.L.7
  • 5
    • 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
  • 6
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur, W. T., Petch, L. A. and Burridge, K. (2000). Integrin engagement suppresses 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
  • 7
    • 0029671074 scopus 로고    scopus 로고
    • Integrin alphavbeta3 mediates chemotactic and haptotactic motility in human melanoma cells through different signaling pathways
    • Aznavoorian, S., Stracke, M. L., Parsons, J., McClanahan, J. and Liotta, L. A. (1996). Integrin alphavbeta3 mediates chemotactic and haptotactic motility in human melanoma cells through different signaling pathways. J. Biol. Chem. 271, 3247-3254.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3247-3254
    • Aznavoorian, S.1    Stracke, M.L.2    Parsons, J.3    McClanahan, J.4    Liotta, L.A.5
  • 9
    • 0035901569 scopus 로고    scopus 로고
    • The F-actin side binding activity of the Arp2/3 complex is essential for actin nucleation and lamellipod extension
    • Bailly, M., Ichetovkin, I., Grant, W., Zebda, N., Machesky, L. M., Segall, J. E. and Condeelis, J. (2001). The F-actin side binding activity of the Arp2/3 complex is essential for actin nucleation and lamellipod extension. Curr. Biol. 11, 620-625.
    • (2001) Curr. Biol. , vol.11 , pp. 620-625
    • Bailly, M.1    Ichetovkin, I.2    Grant, W.3    Zebda, N.4    Machesky, L.M.5    Segall, J.E.6    Condeelis, J.7
  • 10
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg, J. R. (1999). Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185-230.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 11
    • 0032128299 scopus 로고    scopus 로고
    • Modulation of monocyte-endothelial cell interactions by platelet microparticles
    • Barry, O. P., Pratico, D., Savani, R. C. and FitzGerald, G. A. (1998). Modulation of monocyte-endothelial cell interactions by platelet microparticles. J. Clin. Invest. 102, 136-144.
    • (1998) J. Clin. Invest. , vol.102 , pp. 136-144
    • Barry, O.P.1    Pratico, D.2    Savani, R.C.3    FitzGerald, G.A.4
  • 12
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • Berg, J. S. and Cheney, R. E. (2002). Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat. Cell Biol. 4, 246-250.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 13
    • 0030913232 scopus 로고    scopus 로고
    • Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • Black, D. S. and Bliska, J. B. (1997). Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 16, 2730-2744.
    • (1997) EMBO J. , vol.16 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.B.2
  • 14
    • 0033861270 scopus 로고    scopus 로고
    • The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence
    • Black, D. S. and Bliska, J. B. (2000). The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence. Mol. Microbiol. 37, 515-527.
    • (2000) Mol. Microbiol. , vol.37 , pp. 515-527
    • Black, D.S.1    Bliska, J.B.2
  • 15
    • 0033920567 scopus 로고    scopus 로고
    • Interactions between Listeria monocytogenes and host mammalian cells
    • Braun, L. and Cossart, P. (2000). Interactions between Listeria monocytogenes and host mammalian cells. Microbes Infect. 2, 803-811.
    • (2000) Microbes Infect. , vol.2 , pp. 803-811
    • Braun, L.1    Cossart, P.2
  • 16
    • 0037820042 scopus 로고
    • Migration of cells over surfaces
    • New York: Garland Publishing Co
    • Bray, D. (1992). Migration of cells over surfaces. In Cell Movements. pp. 17-29. New York: Garland Publishing Co.
    • (1992) Cell Movements , pp. 17-29
    • Bray, D.1
  • 18
    • 0033975369 scopus 로고    scopus 로고
    • Interaction of enteropathogenic or enterohemorrhagic Escherichia coli with HeLa cells results in translocation of cortactin to the bacterial adherence site
    • Cantarelli, V. V., Takahashi, A., Akeda, Y., Nagayama, K. and Honda, T. (2000). Interaction of enteropathogenic or enterohemorrhagic Escherichia coli with HeLa cells results in translocation of cortactin to the bacterial adherence site. Infect. Immun. 68, 382-386.
    • (2000) Infect. Immun. , vol.68 , pp. 382-386
    • Cantarelli, V.V.1    Takahashi, A.2    Akeda, Y.3    Nagayama, K.4    Honda, T.5
  • 19
  • 20
    • 0032573378 scopus 로고    scopus 로고
    • Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
    • Caron, E. and Hall, A. (1998). Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science 282, 1717-1721.
    • (1998) Science , vol.282 , pp. 1717-1721
    • Caron, E.1    Hall, A.2
  • 21
    • 0032509565 scopus 로고    scopus 로고
    • Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration
    • Cary, L. A., Han, D. C., Polte, T. R., Hanks, S. K. and Guan, J. L. (1998). Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration. J. Cell Biol. 140, 211-221.
    • (1998) J. Cell Biol. , vol.140 , pp. 211-221
    • Cary, L.A.1    Han, D.C.2    Polte, T.R.3    Hanks, S.K.4    Guan, J.L.5
  • 22
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan, A. Y., Bailly, M., Zebda, N., Segall, J. E. and Condeelis, J. S. (2000). Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148, 531-542.
    • (2000) J. Cell Biol. , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 23
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the rho family of GTPases
    • Clark, E. A., King, W. G., Brugge, J. S., Symons, M. and Hynes, R. O. (1998). Integrin-mediated signals regulated by members of the rho family of GTPases. J. Cell Biol. 142, 573-586.
    • (1998) J. Cell Biol. , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 24
    • 0001957916 scopus 로고    scopus 로고
    • The Biochemistry of Animal Cell Crawling
    • New York: Wiley-Liss
    • Condeelis, J. (1998). The Biochemistry of Animal Cell Crawling. In Motion Analysis of Living Cells, pp. 85-100. New York: Wiley-Liss.
    • (1998) Motion Analysis of Living Cells , pp. 85-100
    • Condeelis, J.1
  • 25
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis, J. (2001). How is actin polymerization nucleated in vivo? Trends Cell Biol. 11, 288-293.
    • (2001) Trends Cell Biol. , vol.11 , pp. 288-293
    • Condeelis, J.1
  • 26
    • 0036322385 scopus 로고    scopus 로고
    • Yersinia type III secretion: Send in the effectors
    • Cornelis, G. R. (2002). Yersinia type III secretion: send in the effectors. J. Cell Biol. 158, 401-408.
    • (2002) J. Cell Biol. , vol.158 , pp. 401-408
    • Cornelis, G.R.1
  • 27
    • 0037115488 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
    • Cote, J. F. and Vuori, K. (2002). Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J. Cell Sci. 115, 4901-4913.
    • (2002) J. Cell Sci. , vol.115 , pp. 4901-4913
    • Cote, J.F.1    Vuori, K.2
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • DeMali, K. A., Barlow, C. A. and Burridge, K. (2002). Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891.
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 32
    • 0037032812 scopus 로고    scopus 로고
    • Molecular mechanisms of axon guidance
    • Dickson, B. J. (2002). Molecular mechanisms of axon guidance. Science 298, 1959-1964.
    • (2002) Science , vol.298 , pp. 1959-1964
    • Dickson, B.J.1
  • 33
    • 0032407404 scopus 로고    scopus 로고
    • Intracellular pathogens and the actin cytoskeleton
    • Dramsi, S. and Cossart, P. (1998). Intracellular pathogens and the actin cytoskeleton. Annu. Rev. Cell Dev. Biol. 14, 137-166.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 137-166
    • Dramsi, S.1    Cossart, P.2
  • 35
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden, S., Rohatgi, R., Podtelejnikov, A. V., Mann, M. and Kirschner, M. W. (2002). Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418, 790-793.
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 36
  • 38
    • 0023617861 scopus 로고
    • In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2
    • Gaillard, J. L., Berche, P., Mounier, J., Richard, S. and Sansonetti, P. (1987). In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2. Infect. Immun. 55, 2822-2829.
    • (1987) Infect. Immun. , vol.55 , pp. 2822-2829
    • Gaillard, J.L.1    Berche, P.2    Mounier, J.3    Richard, S.4    Sansonetti, P.5
  • 39
    • 0027535009 scopus 로고
    • A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant
    • Galyov, E. E., Hakansson, S., Forsberg, A. and Wolf-Watz, H. (1993). A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant. Nature 361, 730-732.
    • (1993) Nature , vol.361 , pp. 730-732
    • Galyov, E.E.1    Hakansson, S.2    Forsberg, A.3    Wolf-Watz, H.4
  • 40
    • 0029826289 scopus 로고    scopus 로고
    • Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST
    • Garton, A. J., Flint, A. J. and Tonks, N. K. (1996). Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. Mol. Cell Biol. 16, 6408-6418.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6408-6418
    • Garton, A.J.1    Flint, A.J.2    Tonks, N.K.3
  • 41
    • 0036781979 scopus 로고    scopus 로고
    • How do Rho family GTPases direct axon growth and guidance? A proposal relating signaling pathways to growth cone mechanics
    • Giniger, E. (2002). How do Rho family GTPases direct axon growth and guidance? A proposal relating signaling pathways to growth cone mechanics. Differentiation 70, 385-396.
    • (2002) Differentiation , vol.70 , pp. 385-396
    • Giniger, E.1
  • 42
    • 0035059331 scopus 로고    scopus 로고
    • Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals
    • Goosney, D. L., DeVinney, R. and Finlay, B. B. (2001). Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals. Infect. Immun. 69, 3315-3322.
    • (2001) Infect. Immun. , vol.69 , pp. 3315-3322
    • Goosney, D.L.1    DeVinney, R.2    Finlay, B.B.3
  • 43
    • 0033832890 scopus 로고    scopus 로고
    • Nerve growth factor stimulates coupling of beta1 integrin to distinct transport mechanisms in the filopodia of growth cones
    • Grabham, P. W., Foley, M., Umeojiako, A. and Goldberg, D. J. (2000). Nerve growth factor stimulates coupling of beta1 integrin to distinct transport mechanisms in the filopodia of growth cones. J. Cell Sci. 113, 3003-3012.
    • (2000) J. Cell Sci. , vol.113 , pp. 3003-3012
    • Grabham, P.W.1    Foley, M.2    Umeojiako, A.3    Goldberg, D.J.4
  • 45
    • 0035997135 scopus 로고    scopus 로고
    • Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC)
    • Huang, L., Mittal, B., Sanger, J. W. and Sanger, J. M. (2002). Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC). Cell Motil. Cytoskeleton 52, 255-265.
    • (2002) Cell Motil. Cytoskeleton , vol.52 , pp. 255-265
    • Huang, L.1    Mittal, B.2    Sanger, J.W.3    Sanger, J.M.4
  • 47
    • 0035147433 scopus 로고    scopus 로고
    • Subversion of integrins by enteropathogenic Yersinia
    • Isberg, R. R. and Barnes, P. (2001). Subversion of integrins by enteropathogenic Yersinia. J. Cell Sci. 114, 21-28.
    • (2001) J. Cell Sci. , vol.114 , pp. 21-28
    • Isberg, R.R.1    Barnes, P.2
  • 48
    • 0033920740 scopus 로고    scopus 로고
    • Signaling and invasin-promoted uptake via integrin receptors
    • Isberg, R. R., Hamburger, Z. and Dersch, P. (2000). Signaling and invasin-promoted uptake via integrin receptors. Microbes Infect. 2, 793-801.
    • (2000) Microbes Infect. , vol.2 , pp. 793-801
    • Isberg, R.R.1    Hamburger, Z.2    Dersch, P.3
  • 49
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano, R. L. (2002). Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu. Rev. Pharmacol. Toxicol. 42, 283-323.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 50
    • 0034662928 scopus 로고    scopus 로고
    • A distinctive role for the Yersinia protein kinase: Actin binding, kinase activation, and cytoskeleton disruption
    • Juris, S. J., Rudolph, A. E., Huddler, D., Orth, K. and Dixon, J. E. (2000). A distinctive role for the Yersinia protein kinase: actin binding, kinase activation, and cytoskeleton disruption. Proc. Natl. Acad. Sci. USA 97, 9431-9436.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9431-9436
    • Juris, S.J.1    Rudolph, A.E.2    Huddler, D.3    Orth, K.4    Dixon, J.E.5
  • 52
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., DeVinney, R., Stein, M., Reinscheid, D. J., Frey, E. A. and Finlay, B. B. (1997). Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91, 511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 53
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim, A. S., Kakalis, L. T., Abdul-Manan, N., Liu, G. A. and Rosen, M. K. (2000a). Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404, 151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 54
    • 0034711219 scopus 로고    scopus 로고
    • E-cadherin-mediated cell-cell attachment activates Cdc42
    • Kim, S. H., Li, Z. and Sacks, D. B. (2000b). E-cadherin-mediated cell-cell attachment activates Cdc42. J. Biol. Chem. 275, 36999-37005.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36999-37005
    • Kim, S.H.1    Li, Z.2    Sacks, D.B.3
  • 55
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke, R. L., Leng, J., Molander, R., Brooks, P. C., Vuori, K. and Cheresh, D. A. (1998). CAS/Crk coupling serves as a "molecular switch" for induction of cell migration. J. Cell Biol. 140, 961-972.
    • (1998) J. Cell Biol. , vol.140 , pp. 961-972
    • Klemke, R.L.1    Leng, J.2    Molander, R.3    Brooks, P.C.4    Vuori, K.5    Cheresh, D.A.6
  • 56
    • 0037022538 scopus 로고    scopus 로고
    • Cadherin-directed actin assembly. E-cadherin physically associates with the arp2/3 complex to direct actin assembly in nascent adhesive contacts
    • Kovacs, E. M., Goodwin, M., Ali, R. G., Paterson, A. D. and Yap, A. S. (2002). Cadherin-directed actin assembly. E-cadherin physically associates with the arp2/3 complex to direct actin assembly in nascent adhesive contacts. Curr. Biol. 12, 379-382.
    • (2002) Curr. Biol. , vol.12 , pp. 379-382
    • Kovacs, E.M.1    Goodwin, M.2    Ali, R.G.3    Paterson, A.D.4    Yap, A.S.5
  • 57
    • 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. and Lim, L. (1997). 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. 17, 1201-1211.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 59
    • 0033610810 scopus 로고    scopus 로고
    • Differential effects of integrin alpha chain mutations on invasin and natural ligand interaction
    • Krukonis, E. S., Dersch, P., Eble, J. A. and Isberg, R. R. (1998). Differential effects of integrin alpha chain mutations on invasin and natural ligand interaction. J. Biol. Chem. 273, 31837-31843.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31837-31843
    • Krukonis, E.S.1    Dersch, P.2    Eble, J.A.3    Isberg, R.R.4
  • 60
    • 0027994108 scopus 로고
    • Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly
    • LaFlamme, S. E., Thomas, L. A., Yamada, S. S. and Yamada, K. M. (1994). Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly. J. Cell Biol. 126, 1287-1298.
    • (1994) J. Cell Biol. , vol.126 , pp. 1287-1298
    • LaFlamme, S.E.1    Thomas, L.A.2    Yamada, S.S.3    Yamada, K.M.4
  • 62
    • 0025301659 scopus 로고
    • Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein
    • Leong, J. M., Fournier, R. S. and Isberg, R. R. (1990). Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein. EMBO J. 9, 1979-1989.
    • (1990) EMBO J. , vol.9 , pp. 1979-1989
    • Leong, J.M.1    Fournier, R.S.2    Isberg, R.R.3
  • 63
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • Lommel, S., Benesch, S., Rottner, K., Franz, T., Wehland, J. and Kuhn, R. (2001). Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2, 850-857.
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1    Benesch, S.2    Rottner, K.3    Franz, T.4    Wehland, J.5    Kuhn, R.6
  • 64
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M. and Insall, R. H. (1998). Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 65
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose
    • Machesky, L. M., Atkinson, S. J., Ampe, C., Vandekerckhove, J. and Pollard, T. D. (1994). Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 127, 107-115.
    • (1994) J. Cell Biol. , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 66
    • 0030670302 scopus 로고    scopus 로고
    • Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins
    • Machesky, L. M., Reeves, E., Wientjes, F., Mattheyse, F. J., Grogan, A., Totty, N. F., Burlingame, A. L., Hsuan, J. J. and Segal, A. W. (1997). Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. Biochem. J. 105, 105-112.
    • (1997) Biochem. J. , vol.105 , pp. 105-112
    • Machesky, L.M.1    Reeves, E.2    Wientjes, F.3    Mattheyse, F.J.4    Grogan, A.5    Totty, N.F.6    Burlingame, A.L.7    Hsuan, J.J.8    Segal, A.W.9
  • 68
    • 0031610579 scopus 로고    scopus 로고
    • PAK kinases are directly coupled to the PIX family of nucleotide exchange factors
    • Manser, E., Loo, T. H., Koh, C. G., Zhao, Z. S., Chen, X. Q., Tan, L., Tan, I., Leung, T. and Lim, L. (1998). PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Mol. Cell 1, 183-192.
    • (1998) Mol. Cell , vol.1 , pp. 183-192
    • Manser, E.1    Loo, T.H.2    Koh, C.G.3    Zhao, Z.S.4    Chen, X.Q.5    Tan, L.6    Tan, I.7    Leung, T.8    Lim, L.9
  • 70
    • 0033790639 scopus 로고    scopus 로고
    • Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3
    • May, R. C., Caron, E., Hall, A. and Machesky, L. M. (2000). Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3. Nat. Cell Biol. 2, 246-248.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 246-248
    • May, R.C.1    Caron, E.2    Hall, A.3    Machesky, L.M.4
  • 71
    • 0035976859 scopus 로고    scopus 로고
    • A role for N-WASP in invasin-promoted internalisation
    • McGee, K., Zettl, M., Way, M. and Fallman, M. (2001). A role for N-WASP in invasin-promoted internalisation. FEBS Lett. 509, 59-65.
    • (2001) FEBS Lett. , vol.509 , pp. 59-65
    • McGee, K.1    Zettl, M.2    Way, M.3    Fallman, M.4
  • 72
    • 0029869384 scopus 로고    scopus 로고
    • E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells
    • Mengaud, J., Ohayon, H., Gounon, P., Mege, R. M. and Cossart, P. (1996). E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84, 923-932.
    • (1996) Cell , vol.84 , pp. 923-932
    • Mengaud, J.1    Ohayon, H.2    Gounon, P.3    Mege, R.M.4    Cossart, P.5
  • 73
    • 0032403083 scopus 로고    scopus 로고
    • WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki, H., Suetsugu, S. and Takenawa, T. (1998). WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 17, 6932-6941.
    • (1998) EMBO J. , vol.17 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 74
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki, H., Yamaguchi, H., Suetsugu, S. and Takenawa, T. (2000). IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 408, 732-735.
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 75
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R. D., Heuser, J. A. and Pollard, T. D. (1998). The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95, 6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 76
    • 0034994490 scopus 로고    scopus 로고
    • Recruitment and activation of Rac1 by the formation of E-cadherin-mediated cell-cell adhesion sites
    • Nakagawa, M., Fukata, M., Yamaga, M., Itoh, N. and Kaibuchi, K. (2001). Recruitment and activation of Rac1 by the formation of E-cadherin-mediated cell-cell adhesion sites. J. Cell Sci. 114, 1829-1838.
    • (2001) J. Cell Sci. , vol.114 , pp. 1829-1838
    • Nakagawa, M.1    Fukata, M.2    Yamaga, M.3    Itoh, N.4    Kaibuchi, K.5
  • 77
    • 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., Sasaki, T., Takaishi, K., Kato, M., Yaku, H., Araki, K., Matsuura, Y. and Takai, Y. (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
  • 78
    • 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
  • 80
    • 0034707597 scopus 로고    scopus 로고
    • RhoA function in lamellae formation and migration is regulated by the alpha6beta4 integrin and cAMP metabolism
    • O'Connor, K. L., Nguyen, B. K. and Mercurio, A. M. (2000). RhoA function in lamellae formation and migration is regulated by the alpha6beta4 integrin and cAMP metabolism. J. Cell Biol. 148, 253-258.
    • (2000) J. Cell Biol. , vol.148 , pp. 253-258
    • O'Connor, K.L.1    Nguyen, B.K.2    Mercurio, A.M.3
  • 81
    • 0030978909 scopus 로고    scopus 로고
    • The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
    • Persson, C., Carballeira, N., Wolf-Watz, H. and Fallman, M. (1997). The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 16, 2307-2318.
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fallman, M.4
  • 82
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • Price, L. S., Leng, J., Schwartz, M. A. and Bokoch, G. M. (1998). Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol. Biol. Cell 9, 1863-1871.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1863-1871
    • Price, L.S.1    Leng, J.2    Schwartz, M.A.3    Bokoch, G.M.4
  • 83
    • 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
  • 84
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X. D., Kiosses, W. B., Sieg, D. J., Otey, C. A., Schlaepfer, D. D. and Schwartz, M. A. (2000). Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 1679-1684.
    • (2000) J. Cell Sci. , vol.113 , pp. 1679-1684
    • Ren, X.D.1    Kiosses, W.B.2    Sieg, D.J.3    Otey, C.A.4    Schlaepfer, D.D.5    Schwartz, M.A.6
  • 86
    • 0029933731 scopus 로고    scopus 로고
    • A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation
    • Rosenshine, I., Ruschkowski, S., Stein, M., Reinscheid, D. J., Mills, S. D. and Finlay, B. B. (1996). A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation. EMBO J. 15, 2613-2624.
    • (1996) EMBO J. , vol.15 , pp. 2613-2624
    • Rosenshine, I.1    Ruschkowski, S.2    Stein, M.3    Reinscheid, D.J.4    Mills, S.D.5    Finlay, B.B.6
  • 87
    • 0023711836 scopus 로고
    • Inhibition of phagocytosis in Yersinia pseudotuberculosis: A virulence plasmid-encoded ability involving the Yop2b protein
    • Rosqvist, R., Bolin, I. and Wolf-Watz, H. (1988). Inhibition of phagocytosis in Yersinia pseudotuberculosis: a virulence plasmid-encoded ability involving the Yop2b protein. Infect. Immun. 56, 2139-2143.
    • (1988) Infect. Immun. , vol.56 , pp. 2139-2143
    • Rosqvist, R.1    Bolin, I.2    Wolf-Watz, H.3
  • 88
    • 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
  • 89
    • 0037113097 scopus 로고    scopus 로고
    • PTP-PEST controls motility through regulation of Rac1
    • Sastry, S. K., Lyons, P. D., Schaller, M. D. and Burridge, K. (2002). PTP-PEST controls motility through regulation of Rac1. J. Cell Sci. 115, 4305-4316.
    • (2002) J. Cell Sci. , vol.115 , pp. 4305-4316
    • Sastry, S.K.1    Lyons, P.D.2    Schaller, M.D.3    Burridge, K.4
  • 90
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • 1540
    • Schaller, M. D. (2001). Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim. Biophys. Acta 1540, 1-21.
    • (2001) Biochim. Biophys. Acta , pp. 1-21
    • Schaller, M.D.1
  • 91
    • 0031877683 scopus 로고    scopus 로고
    • Microinjection of protein tyrosine phosphatases into fibroblasts disrupts focal adhesions and stress fibers
    • Schneider, G. B., Gilmore, A. P., Lohse, D. L., Romer, L. H. and Burridge, K. (1998). Microinjection of protein tyrosine phosphatases into fibroblasts disrupts focal adhesions and stress fibers. Cell Adhes. Commun. 5, 207-219.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 207-219
    • Schneider, G.B.1    Gilmore, A.P.2    Lohse, D.L.3    Romer, L.H.4    Burridge, K.5
  • 92
    • 0037417878 scopus 로고    scopus 로고
    • Biochemical characterization of the Yersinia YopT protease: Cleavage site and recognition elements in Rho GTPases
    • Shao, F., Vacratsis, P. O., Bao, Z., Bowers, K. E., Fierke, C. A. and Dixon, J. E. (2003). Biochemical characterization of the Yersinia YopT protease: Cleavage site and recognition elements in Rho GTPases. Proc. Natl. Acad. Sci. USA 100, 904-909.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 904-909
    • Shao, F.1    Vacratsis, P.O.2    Bao, Z.3    Bowers, K.E.4    Fierke, C.A.5    Dixon, J.E.6
  • 93
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R. J., Henry, M., Solomon, F. and Jacks, T. (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
  • 94
    • 0032513047 scopus 로고    scopus 로고
    • Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin
    • Shen, Y., Schneider, G., Cloutier, J. F., Veillette, A. and Schaller, M. D. (1998). Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin. J. Biol. Chem. 273, 6474-6481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6474-6481
    • Shen, Y.1    Schneider, G.2    Cloutier, J.F.3    Veillette, A.4    Schaller, M.D.5
  • 95
    • 0037084459 scopus 로고    scopus 로고
    • N-WASP activation by a beta1-integrin-dependent mechanism supports PI3K-independent chemotaxis stimulated by urokinase-type plasminogen activator
    • Sturge, J., Hamelin, J. and Jones, G. E. (2002). N-WASP activation by a beta1-integrin-dependent mechanism supports PI3K-independent chemotaxis stimulated by urokinase-type plasminogen activator. J. Cell Sci. 115, 699-711.
    • (2002) J. Cell Sci. , vol.115 , pp. 699-711
    • Sturge, J.1    Hamelin, J.2    Jones, G.E.3
  • 96
    • 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
  • 97
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: Mechanism of cell body translocation
    • Svitkina, T. M., Verkhovsky, A. B., McQuade, K. M. and Borisy, G. G. (1997). Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J. Cell Biol. 139, 397-415.
    • (1997) J. Cell Biol. , vol.139 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 102
    • 0034097414 scopus 로고    scopus 로고
    • GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: A mechanism for disruption of actin microfilament structure
    • Von Pawel-Rammingen, U., Telepnev, M. V., Schmidt, G., Aktories, K., Wolf-Watz, H. and Rosqvist, R. (2000). GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure. Mol. Microbiol. 36, 737-748.
    • (2000) Mol. Microbiol. , vol.36 , pp. 737-748
    • Von Pawel-Rammingen, U.1    Telepnev, M.V.2    Schmidt, G.3    Aktories, K.4    Wolf-Watz, H.5    Rosqvist, R.6
  • 103
    • 0028981376 scopus 로고
    • Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix
    • Vuori, K. and Ruoslahti, E. (1995). Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix. J. Biol. Chem. 270, 22259-22262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22259-22262
    • Vuori, K.1    Ruoslahti, E.2
  • 104
    • 0029664531 scopus 로고    scopus 로고
    • Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Vuori, K., Hirai, H., Aizawa, S. and Ruoslahti, E. (1996). Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol. Cell Biol. 16, 2606-2613.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 105
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • Weed, S. A., Karginov, A. V., Schafer, D. A., Weaver, A. M., Kinley, A. W., Cooper, J. A. and Parsons, J. T. (2000). Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151, 29-40.
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 106
    • 0031610209 scopus 로고    scopus 로고
    • Purification and assay of the platelet Arp2/3 complex
    • Welch, M. D. and Mitchison, T. J. (1998). Purification and assay of the platelet Arp2/3 complex. Methods Enzymol. 298, 52-61.
    • (1998) Methods Enzymol. , vol.298 , pp. 52-61
    • Welch, M.D.1    Mitchison, T.J.2
  • 107
    • 0030802671 scopus 로고    scopus 로고
    • The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly
    • Welch, M. D., DePace, A. H., Verma, S., Iwamatsu, A. and Mitchison, T. J. (1997). The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. J. Cell Biol. 138, 375-384.
    • (1997) J. Cell Biol. , vol.138 , pp. 375-384
    • Welch, M.D.1    DePace, A.H.2    Verma, S.3    Iwamatsu, A.4    Mitchison, T.J.5
  • 108
    • 0034775391 scopus 로고    scopus 로고
    • Yersinia enterocolitica invasin triggers phagocytosis via beta1 integrins, CDC42Hs and WASp in macrophages
    • Wiedemann, A., Linder, S., Grassl, G., Albert, M., Autenrieth, I. and Aepfelbacher, M. (2001). Yersinia enterocolitica invasin triggers phagocytosis via beta1 integrins, CDC42Hs and WASp in macrophages. Cell Microbiol. 3, 693-702.
    • (2001) Cell Microbiol. , vol.3 , pp. 693-702
    • Wiedemann, A.1    Linder, S.2    Grassl, G.3    Albert, M.4    Autenrieth, I.5    Aepfelbacher, M.6
  • 109
    • 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
  • 110
    • 0037421188 scopus 로고    scopus 로고
    • Direct cadherin-activated cell signaling: A view from the plasma membrane
    • Yap, A. S. and Kovacs, E. M. (2003). Direct cadherin-activated cell signaling: a view from the plasma membrane. J. Cell Biol 160, 11-16.
    • (2003) J. Cell Biol. , vol.160 , pp. 11-16
    • Yap, A.S.1    Kovacs, E.M.2
  • 111
    • 0028930717 scopus 로고
    • Mutation of the cytoplasmic domain of the integrin beta 3 subunit. Differential effects on cell spreading, recruitment to adhesion plaques, endocytosis, and phagocytosis
    • Ylanne, J., Huuskonen, J., O'Toole, T. E., Ginsberg, M. H., Virtanen, I. and Gahmberg, C. G. (1995). Mutation of the cytoplasmic domain of the integrin beta 3 subunit. Differential effects on cell spreading, recruitment to adhesion plaques, endocytosis, and phagocytosis. J. Biol. Chem. 270, 9550-9557.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9550-9557
    • Ylanne, J.1    Huuskonen, J.2    O'Toole, T.E.3    Ginsberg, M.H.4    Virtanen, I.5    Gahmberg, C.G.6
  • 112
    • 0034757893 scopus 로고    scopus 로고
    • Components of cell-matrix adhesions
    • Zamir, E. and Geiger, B. (2001a). Components of cell-matrix adhesions. J. Cell Sci. 114, 3577-3579.
    • (2001) J. Cell Sci. , vol.114 , pp. 3577-3579
    • Zamir, E.1    Geiger, B.2
  • 113
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E. and Geiger, B. (2001b). Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114, 3583-3590.
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 114
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension
    • Zebda, N., Bernard, O., Bailly, M., Welti, S., Lawrence, D. S. and Condeelis, J. S. (2000). Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension. J. Cell Biol. 151, 1119-1128.
    • (2000) J. Cell Biol. , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 115
    • 0037421205 scopus 로고    scopus 로고
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng, L., Si, X., Yu, W. P., Le, H. T., Ng, K. P., Teng, R. M., Ryan, K., Wang, D. Z., Ponniah, S. and Pallen, C. J. (2003). PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 160, 137-146.
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6    Ryan, K.7    Wang, D.Z.8    Ponniah, S.9    Pallen, C.J.10
  • 116
    • 0027058169 scopus 로고
    • Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase
    • Zhang, Z. Y., Clemens, J. C., Schubert, H. L., Stuckey, J. A., Fischer, M. W., Hume, D. M., Saper, M. A. and Dixon, J. E. (1992). Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase. J. Biol. Chem. 267, 23759-23766.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23759-23766
    • Zhang, Z.Y.1    Clemens, J.C.2    Schubert, H.L.3    Stuckey, J.A.4    Fischer, M.W.5    Hume, D.M.6    Saper, M.A.7    Dixon, J.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.