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Volumn 126, Issue 20, 2013, Pages 4572-4588

Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation

Author keywords

Actin; Adhesion; CAAX; Chemotaxis; Filopodia; Lamellipodia; Migration; Rac1

Indexed keywords

RAC PROTEIN; RAC1 PROTEIN; RAC2 PROTEIN; RAC3 PROTEIN; UNCLASSIFIED DRUG;

EID: 84885454469     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.118232     Document Type: Article
Times cited : (123)

References (74)
  • 1
    • 0942268723 scopus 로고    scopus 로고
    • Rho GTPases have diverse effects on the organization of the actin filament system
    • Aspenström, P., Fransson, A. and Saras, J. (2004). Rho GTPases have diverse effects on the organization of the actin filament system. Biochem. J. 377, 327-337.
    • (2004) Biochem. J. , vol.377 , pp. 327-337
    • Aspenström, P.1    Fransson, A.2    Saras, J.3
  • 2
    • 11844280881 scopus 로고    scopus 로고
    • The Cool-2/alpha-Pix protein mediates a Cdc42-Rac signaling cascade
    • Baird, D., Feng, Q. and Cerione, R. A. (2005). The Cool-2/alpha-Pix protein mediates a Cdc42-Rac signaling cascade. Curr. Biol. 15, 1-10.
    • (2005) Curr. Biol. , vol.15 , pp. 1-10
    • Baird, D.1    Feng, Q.2    Cerione, R.A.3
  • 3
    • 0037020265 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-biphosphate (PIP2)- induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2
    • Benesch, S., Lommel, S., Steffen, A., Stradal, T. E., Scaplehorn, N., Way, M., Wehland, J. and Rottner, K. (2002). Phosphatidylinositol 4,5-biphosphate (PIP2)- induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2. J. Biol. Chem. 277, 37771-37776.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37771-37776
    • Benesch, S.1    Lommel, S.2    Steffen, A.3    Stradal, T.E.4    Scaplehorn, N.5    Way, M.6    Wehland, J.7    Rottner, K.8
  • 4
    • 84865957893 scopus 로고    scopus 로고
    • Cell mechanics control rapid transitions between blebs and lamellipodia during migration
    • Bergert, M., Chandradoss, S. D., Desai, R. A. and Paluch, E. (2012). Cell mechanics control rapid transitions between blebs and lamellipodia during migration. Proc. Natl. Acad. Sci. USA 109, 14434-14439.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14434-14439
    • Bergert, M.1    Chandradoss, S.D.2    Desai, R.A.3    Paluch, E.4
  • 5
    • 0345305736 scopus 로고    scopus 로고
    • Differential distribution of Rac1 and Rac3 GTPases in the developing mouse brain: implications for a role of Rac3 in Purkinje cell differentiation
    • Bolis, A., Corbetta, S., Cioce, A. and de Curtis, I. (2003). Differential distribution of Rac1 and Rac3 GTPases in the developing mouse brain: implications for a role of Rac3 in Purkinje cell differentiation. Eur. J. Neurosci. 18, 2417-2424.
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 2417-2424
    • Bolis, A.1    Corbetta, S.2    Cioce, A.3    de Curtis, I.4
  • 6
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk, V. L., Ashby, M. N. and Rine, J. (1997). Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275, 1796-1800.
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 7
    • 0033166687 scopus 로고    scopus 로고
    • Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands
    • Carl, U. D., Pollmann, M., Orr, E., Gertlere, F. B., Chakraborty, T. and Wehland, J. (1999). Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands. Curr. Biol. 9, 715-718.
    • (1999) Curr. Biol. , vol.9 , pp. 715-718
    • Carl, U.D.1    Pollmann, M.2    Orr, E.3    Gertlere, F.B.4    Chakraborty, T.5    Wehland, J.6
  • 9
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C. K., Vicente-Manzanares, M., Zareno, J., Whitmore, L. A., Mogilner, A. and Horwitz, A. R. (2008). Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 10, 1039-1050.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 12
    • 26244449496 scopus 로고    scopus 로고
    • Cdc42 is not essential for filopodium formation, directed migration, cell polarization, and mitosis in fibroblastoid cells
    • Czuchra, A., Wu, X., Meyer, H., van Hengel, J., Schroeder, T., Geffers, R., Rottner, K. and Brakebusch, C. (2005). Cdc42 is not essential for filopodium formation, directed migration, cell polarization, and mitosis in fibroblastoid cells. Mol. Biol. Cell 16, 4473-4484.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4473-4484
    • Czuchra, A.1    Wu, X.2    Meyer, H.3    van Hengel, J.4    Schroeder, T.5    Geffers, R.6    Rottner, K.7    Brakebusch, C.8
  • 14
    • 0035234218 scopus 로고    scopus 로고
    • Gene targeting in ES cells
    • DeChiara, T. M. (2001). Gene targeting in ES cells. Methods Mol. Biol. 158, 19-45.
    • (2001) Methods Mol. Biol. , vol.158 , pp. 19-45
    • DeChiara, T.M.1
  • 15
    • 76549123909 scopus 로고    scopus 로고
    • Generation of branched actin networks: assembly and regulation of the N-WASP and WAVE molecular machines
    • Derivery, E. and Gautreau, A. (2010). Generation of branched actin networks: assembly and regulation of the N-WASP and WAVE molecular machines. Bioessays 32, 119-131.
    • (2010) Bioessays , vol.32 , pp. 119-131
    • Derivery, E.1    Gautreau, A.2
  • 16
    • 0024425981 scopus 로고
    • rac, a novel ras-related family of proteins that are botulinum toxin substrates
    • Didsbury, J., Weber, R. F., Bokoch, G. M., Evans, T. and Snyderman, R. (1989). rac, a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264, 16378-16382.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16378-16382
    • Didsbury, J.1    Weber, R.F.2    Bokoch, G.M.3    Evans, T.4    Snyderman, R.5
  • 17
    • 33847311403 scopus 로고    scopus 로고
    • Formins regulate the actin-related protein 2/3 complexindependent polarization of the centrosome to the immunological synapse
    • Gomez, T. S., Kumar, K., Medeiros, R. B., Shimizu, Y., Leibson, P. J. and Billadeau, D. D. (2007). Formins regulate the actin-related protein 2/3 complexindependent polarization of the centrosome to the immunological synapse. Immunity 26, 177-190.
    • (2007) Immunity , vol.26 , pp. 177-190
    • Gomez, T.S.1    Kumar, K.2    Medeiros, R.B.3    Shimizu, Y.4    Leibson, P.J.5    Billadeau, D.D.6
  • 18
    • 33745833345 scopus 로고    scopus 로고
    • Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly
    • Guo, F., Debidda, M., Yang, L., Williams, D. A. and Zheng, Y. (2006). Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly. J. Biol. Chem. 281, 18652-18659.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18652-18659
    • Guo, F.1    Debidda, M.2    Yang, L.3    Williams, D.A.4    Zheng, Y.5
  • 19
    • 0035896436 scopus 로고    scopus 로고
    • Scar/WAVE is localised at the tips of protruding lamellipodia in living cells
    • Hahne, P., Sechi, A., Benesch, S. and Small, J. V. (2001). Scar/WAVE is localised at the tips of protruding lamellipodia in living cells. FEBS Lett. 492, 215-220.
    • (2001) FEBS Lett. , vol.492 , pp. 215-220
    • Hahne, P.1    Sechi, A.2    Benesch, S.3    Small, J.V.4
  • 20
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman, S. J. and Ridley, A. J. (2008). Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 9, 690-701.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 21
    • 0025906597 scopus 로고
    • Post-translational modifications of the Cterminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins
    • Hori, Y., Kikuchi, A., Isomura, M., Katayama, M., Miura, Y., Fujioka, H., Kaibuchi, K. and Takai, Y. (1991). Post-translational modifications of the Cterminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene 6, 515- 522.
    • (1991) Oncogene , vol.6
    • Hori, Y.1    Kikuchi, A.2    Isomura, M.3    Katayama, M.4    Miura, Y.5    Fujioka, H.6    Kaibuchi, K.7    Takai, Y.8
  • 24
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • Iwasa, J. H. and Mullins, R. D. (2007). Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly. Curr. Biol. 17, 395-406.
    • (2007) Curr. Biol. , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.D.2
  • 25
    • 0042674398 scopus 로고    scopus 로고
    • RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo
    • Katoh, H. and Negishi, M. (2003). RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo. Nature 424, 461-464.
    • (2003) Nature , vol.424 , pp. 461-464
    • Katoh, H.1    Negishi, M.2
  • 28
    • 0242286595 scopus 로고    scopus 로고
    • Abi, Sra1, and Kette control the stability and localization of SCAR/WAVE to regulate the formation of actin-based protrusions
    • Kunda, P., Craig, G., Dominguez, V. and Baum, B. (2003). Abi, Sra1, and Kette control the stability and localization of SCAR/WAVE to regulate the formation of actin-based protrusions. Curr. Biol. 13, 1867-1875.
    • (2003) Curr. Biol. , vol.13 , pp. 1867-1875
    • Kunda, P.1    Craig, G.2    Dominguez, V.3    Baum, B.4
  • 29
    • 44449097488 scopus 로고    scopus 로고
    • On the Rho'd: the regulation of membrane protrusions by Rho-GTPases
    • Ladwein, M. and Rottner, K. (2008). On the Rho'd: the regulation of membrane protrusions by Rho-GTPases. FEBS Lett. 582, 2066-2074.
    • (2008) FEBS Lett. , vol.582 , pp. 2066-2074
    • Ladwein, M.1    Rottner, K.2
  • 32
    • 70449112591 scopus 로고    scopus 로고
    • Activation of the WAVE complex by coincident signals controls actin assembly
    • Lebensohn, A. M. and Kirschner, M. W. (2009). Activation of the WAVE complex by coincident signals controls actin assembly. Mol. Cell 36, 512-524.
    • (2009) Mol. Cell , vol.36 , pp. 512-524
    • Lebensohn, A.M.1    Kirschner, M.W.2
  • 33
    • 33644901594 scopus 로고    scopus 로고
    • Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells
    • Lele, T. P., Pendse, J., Kumar, S., Salanga, M., Karavitis, J. and Ingber, D. E. (2006). Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells. J. Cell. Physiol. 207, 187-194.
    • (2006) J. Cell. Physiol. , vol.207 , pp. 187-194
    • Lele, T.P.1    Pendse, J.2    Kumar, S.3    Salanga, M.4    Karavitis, J.5    Ingber, D.E.6
  • 34
    • 65649134364 scopus 로고    scopus 로고
    • Rac1 expression by fibroblasts is required for tissue repair in vivo
    • Liu, S., Kapoor, M. and Leask, A. (2009). Rac1 expression by fibroblasts is required for tissue repair in vivo. Am. J. Pathol. 174, 1847-1856.
    • (2009) Am. J. Pathol. , vol.174 , pp. 1847-1856
    • Liu, S.1    Kapoor, M.2    Leask, A.3
  • 35
    • 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 Kühn, 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    Kühn, R.6
  • 36
    • 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
  • 37
    • 47649088106 scopus 로고    scopus 로고
    • Endogenous RhoG is dispensable for integrin-mediated cell spreading but contributes to Rac-independent migration
    • Meller, J., Vidali, L. and Schwartz, M. A. (2008). Endogenous RhoG is dispensable for integrin-mediated cell spreading but contributes to Rac-independent migration. J. Cell Sci. 121, 1981-1989.
    • (2008) J. Cell Sci. , vol.121 , pp. 1981-1989
    • Meller, J.1    Vidali, L.2    Schwartz, M.A.3
  • 39
    • 33845700946 scopus 로고    scopus 로고
    • Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing
    • Miyoshi, T., Tsuji, T., Higashida, C., Hertzog, M., Fujita, A., Narumiya, S., Scita, G. and Watanabe, N. (2006). Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing. J. Cell Biol. 175, 947-955.
    • (2006) J. Cell Biol. , vol.175 , pp. 947-955
    • Miyoshi, T.1    Tsuji, T.2    Higashida, C.3    Hertzog, M.4    Fujita, A.5    Narumiya, S.6    Scita, G.7    Watanabe, N.8
  • 40
    • 66349125397 scopus 로고    scopus 로고
    • Cdc42 and Rac family GTPases regulate mode and speed but not direction of primary fibroblast migration during platelet-derived growth factordependent chemotaxis
    • Monypenny, J., Zicha, D., Higashida, C., Oceguera-Yanez, F., Narumiya, S. and Watanabe, N. (2009). Cdc42 and Rac family GTPases regulate mode and speed but not direction of primary fibroblast migration during platelet-derived growth factordependent chemotaxis. Mol. Cell. Biol. 29, 2730-2747.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2730-2747
    • Monypenny, J.1    Zicha, D.2    Higashida, C.3    Oceguera-Yanez, F.4    Narumiya, S.5    Watanabe, N.6
  • 42
    • 41549108457 scopus 로고    scopus 로고
    • Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella
    • Nemethova, M., Auinger, S. and Small, J. V. (2008). Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella. J. Cell Biol. 180, 1233-1244.
    • (2008) J. Cell Biol. , vol.180 , pp. 1233-1244
    • Nemethova, M.1    Auinger, S.2    Small, J.V.3
  • 43
    • 55549116027 scopus 로고    scopus 로고
    • Arp2 depletion inhibits sheet-like protrusions but not linear protrusions of fibroblasts and lymphocytes
    • Nicholson-Dykstra, S. M. and Higgs, H. N. (2008). Arp2 depletion inhibits sheet-like protrusions but not linear protrusions of fibroblasts and lymphocytes. Cell Motil. Cytoskeleton 65, 904-922.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 904-922
    • Nicholson-Dykstra, S.M.1    Higgs, H.N.2
  • 45
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. and Hall, A. (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 46
    • 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
  • 47
    • 79551560265 scopus 로고    scopus 로고
    • The perplexing case of the geranylgeranyl transferase-deficient mouse
    • Philips, M. R. (2011). The perplexing case of the geranylgeranyl transferase-deficient mouse. J. Clin. Invest. 121, 510-513.
    • (2011) J. Clin. Invest. , vol.121 , pp. 510-513
    • Philips, M.R.1
  • 48
    • 77957223013 scopus 로고    scopus 로고
    • Mechanisms of force generation and force transmission during interstitial leukocyte migration
    • Renkawitz, J. and Sixt, M. (2010). Mechanisms of force generation and force transmission during interstitial leukocyte migration. EMBO Rep. 11, 744-750.
    • (2010) EMBO Rep. , vol.11 , pp. 744-750
    • Renkawitz, J.1    Sixt, M.2
  • 49
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley, A. J. (2006). Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16, 522-529.
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 50
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. and Hall, A. (1992). The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 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
  • 51
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • Rogers, S. L., Wiedemann, U., Stuurman, N. and Vale, R. D. (2003). Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J. Cell Biol. 162, 1079-1088.
    • (2003) J. Cell Biol. , vol.162 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 52
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T. and Kirschner, M. W. (1999). The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 53
    • 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. (1999a). 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
  • 55
    • 0035162704 scopus 로고    scopus 로고
    • Zyxin is not colocalized with vasodilator-stimulated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions
    • Rottner, K., Krause, M., Gimona, M., Small, J. V. and Wehland, J. (2001). Zyxin is not colocalized with vasodilator-stimulated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions. Mol. Biol. Cell 12, 3103-3113.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3103-3113
    • Rottner, K.1    Krause, M.2    Gimona, M.3    Small, J.V.4    Wehland, J.5
  • 57
    • 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
  • 60
    • 0036024856 scopus 로고    scopus 로고
    • RhoA biological activity is dependent on prenylation but independent of specific isoprenoid modification
    • Solski, P. A., Helms, W., Keely, P. J., Su, L. and Der, C. J. (2002). RhoA biological activity is dependent on prenylation but independent of specific isoprenoid modification. Cell Growth Differ. 13, 363-373
    • (2002) Cell Growth Differ. , vol.13 , pp. 363-373
    • Solski, P.A.1    Helms, W.2    Keely, P.J.3    Su, L.4    Der, C.J.5
  • 63
    • 30844466190 scopus 로고    scopus 로고
    • Protein complexes regulating Arp2/3-mediated actin assembly
    • Stradal, T. E. and Scita, G. (2006). Protein complexes regulating Arp2/3-mediated actin assembly. Curr. Opin. Cell Biol. 18, 4-10.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 4-10
    • Stradal, T.E.1    Scita, G.2
  • 64
    • 0035811020 scopus 로고    scopus 로고
    • The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia
    • Stradal, T., Courtney, K. D., Rottner, K., Hahne, P., Small, J. V. and Pendergast, A. M. (2001). The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia. Curr. Biol. 11, 891-895.
    • (2001) Curr. Biol. , vol.11 , pp. 891-895
    • Stradal, T.1    Courtney, K.D.2    Rottner, K.3    Hahne, P.4    Small, J.V.5    Pendergast, A.M.6
  • 66
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni, P., Rubinstein, B., Unruh, J. R., Durnin, M., Hanein, D. and Li, R. (2012). The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration. J. Cell Biol. 197, 239-251.
    • (2012) J. Cell Biol. , vol.197 , pp. 239-251
    • Suraneni, P.1    Rubinstein, B.2    Unruh, J.R.3    Durnin, M.4    Hanein, D.5    Li, R.6
  • 67
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
    • Takenawa, T. and Suetsugu, S. (2007). The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 8, 37-48.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 68
    • 0032518164 scopus 로고    scopus 로고
    • Efficient production of Cre-mediated site-directed recombinants through the utilization of the puromycin resistance gene, pac: a transient gene-integration marker for ES cells
    • Taniguchi, M., Sanbo, M., Watanabe, S., Naruse, I., Mishina, M. and Yagi, T. (1998). Efficient production of Cre-mediated site-directed recombinants through the utilization of the puromycin resistance gene, pac: a transient gene-integration marker for ES cells. Nucleic Acids Res. 26, 679-680.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 679-680
    • Taniguchi, M.1    Sanbo, M.2    Watanabe, S.3    Naruse, I.4    Mishina, M.5    Yagi, T.6
  • 69
    • 33745751364 scopus 로고    scopus 로고
    • Rac1-null mouse embryonic fibroblasts are motile and respond to platelet-derived growth factor
    • Vidali, L., Chen, F., Cicchetti, G., Ohta, Y. and Kwiatkowski, D. J. (2006). Rac1-null mouse embryonic fibroblasts are motile and respond to platelet-derived growth factor. Mol. Biol. Cell 17, 2377-2390.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2377-2390
    • Vidali, L.1    Chen, F.2    Cicchetti, G.3    Ohta, Y.4    Kwiatkowski, D.J.5
  • 71
    • 79955538660 scopus 로고    scopus 로고
    • Actomyosingenerated tension controls the molecular kinetics of focal adhesions
    • Wolfenson, H., Bershadsky, A., Henis, Y. I. and Geiger, B. (2011). Actomyosingenerated tension controls the molecular kinetics of focal adhesions. J. Cell Sci. 124, 1425-1432.
    • (2011) J. Cell Sci. , vol.124 , pp. 1425-1432
    • Wolfenson, H.1    Bershadsky, A.2    Henis, Y.I.3    Geiger, B.4
  • 72
    • 33845999824 scopus 로고    scopus 로고
    • Yersinia pseudotuberculosis spatially controls activation and misregulation of host cell Rac1
    • Wong, K. W. and Isberg, R. R. (2005). Yersinia pseudotuberculosis spatially controls activation and misregulation of host cell Rac1. PLoS Pathog. 1, e16.
    • (2005) PLoS Pathog. , vol.1
    • Wong, K.W.1    Isberg, R.R.2
  • 73
    • 84863229890 scopus 로고    scopus 로고
    • Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis
    • Wu, C., Asokan, S. B., Berginski, M. E., Haynes, E. M., Sharpless, N. E., Griffith, J. D., Gomez, S. M. and Bear, J. E. (2012). Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis. Cell 148, 973- 987.
    • (2012) Cell , vol.148
    • Wu, C.1    Asokan, S.B.2    Berginski, M.E.3    Haynes, E.M.4    Sharpless, N.E.5    Griffith, J.D.6    Gomez, S.M.7    Bear, J.E.8
  • 74
    • 80052472031 scopus 로고    scopus 로고
    • Visualizing branched actin filaments in lamellipodia by electron tomography
    • author reply 1013-1014
    • Yang, C. and Svitkina, T. (2011). Visualizing branched actin filaments in lamellipodia by electron tomography. Nat. Cell Biol. 13, 1012-1013, author reply 1013-1014.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1012-1013
    • Yang, C.1    Svitkina, T.2


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