메뉴 건너뛰기




Volumn 24, Issue 18, 2013, Pages 2861-2875

Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; COFILIN; COMPLEMENTARY DNA; ENHANCED GREEN FLUORESCENT PROTEIN; ENHANCED YELLOW FLUORESCENT PROTEIN; MYOSIN; PYRENE; RAC1 PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; WAVE PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 84884479460     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-12-0857     Document Type: Article
Times cited : (63)

References (92)
  • 1
    • 0034698675 scopus 로고    scopus 로고
    • Stimulation of fascin spikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc42
    • DOI 10.1083/jcb.150.4.807
    • Adams JC, Schwartz MA (2000). Stimulation of fascin spikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc42. J Cell Biol 150, 807-822. (Pubitemid 30663417)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 807-822
    • Adams, J.C.1    Schwartz, M.A.2
  • 2
    • 35348869727 scopus 로고    scopus 로고
    • Cordon-Bleu Is an Actin Nucleation Factor and Controls Neuronal Morphology
    • DOI 10.1016/j.cell.2007.08.030, PII S0092867407010938
    • Ahuja R, Pinyol R, Reichenbach N, Custer L, Klingensmith J, Kessels MM, Qualmann B (2007). Cordon-bleu is an actin nucleation factor and controls neuronal morphology. Cell 131, 337-350. (Pubitemid 47592919)
    • (2007) Cell , vol.131 , Issue.2 , pp. 337-350
    • Ahuja, R.1    Pinyol, R.2    Reichenbach, N.3    Custer, L.4    Klingensmith, J.5    Kessels, M.M.6    Qualmann, B.7
  • 3
    • 43949143882 scopus 로고    scopus 로고
    • Capping Protein Increases the Rate of Actin-Based Motility by Promoting Filament Nucleation by the Arp2/3 Complex
    • DOI 10.1016/j.cell.2008.04.011, PII S0092867408004984
    • Akin O, Mullins RD (2008). Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complex. Cell 133, 841-851. (Pubitemid 351707682)
    • (2008) Cell , vol.133 , Issue.5 , pp. 841-851
    • Akin, O.1    Mullins, R.D.2
  • 4
    • 0029761790 scopus 로고    scopus 로고
    • Coordination of protrusion and translocation of the keratocyte involves rolling of the cell body
    • Anderson KI, Wang YL, Small JV (1996). Coordination of protrusion and translocation of the keratocyte involves rolling of the cell body. J Cell Biol 134, 1209-1218. (Pubitemid 26300166)
    • (1996) Journal of Cell Biology , vol.134 , Issue.5 , pp. 1209-1218
    • Anderson, K.I.1    Wang, Y.-L.2    Small, J.V.3
  • 5
    • 46249128115 scopus 로고    scopus 로고
    • Correlated light and electron microscopy of the cytoskeleton
    • Auinger S, Small JV (2008). Correlated light and electron microscopy of the cytoskeleton. Methods Cell Biol 88, 257-272.
    • (2008) Methods Cell Biol , vol.88 , pp. 257-272
    • Auinger, S.1    Small, J.V.2
  • 6
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein BW, Bamburg JR (1982). Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil 2, 1-8. (Pubitemid 12150935)
    • (1982) Cell Motility , vol.2 , Issue.1 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 7
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein BW, Bamburg JR (2010). ADF/cofilin: a functional node in cell biology. Trends Cell Biol 20, 187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 8
    • 84861851966 scopus 로고    scopus 로고
    • FMNL2 drives actin-based protrusion and migration downstream of Cdc42
    • Block J et al. (2012). FMNL2 drives actin-based protrusion and migration downstream of Cdc42. Curr Biol 22, 1005-1012.
    • (2012) Curr Biol , vol.22 , pp. 1005-1012
    • Block, J.1
  • 11
    • 75649129741 scopus 로고    scopus 로고
    • How tropomyosin regulates lamellipodial actin-based motility: A combined biochemical and reconstituted motility approach
    • Bugyi B, Didry D, Carlier MF (2010). How tropomyosin regulates lamellipodial actin-based motility: a combined biochemical and reconstituted motility approach. EMBO J 29, 14-26.
    • (2010) EMBO J , vol.29 , pp. 14-26
    • Bugyi, B.1    Didry, D.2    Carlier, M.F.3
  • 13
    • 46149096223 scopus 로고    scopus 로고
    • WHAMM Is an Arp2/3 Complex Activator That Binds Microtubules and Functions in ER to Golgi Transport
    • DOI 10.1016/j.cell.2008.05.032, PII S0092867408006934
    • Campellone KG, Webb NJ, Znameroski EA, Welch MD (2008). WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 134, 148-161. (Pubitemid 351905739)
    • (2008) Cell , vol.134 , Issue.1 , pp. 148-161
    • Campellone, K.G.1    Webb, N.J.2    Znameroski, E.A.3    Welch, M.D.4
  • 14
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • Campellone KG, Welch MD (2010). A nucleator arms race: cellular control of actin assembly. Nat Rev Mol Cell Biol 11, 237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 17
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: Matching assembly factors with cellular structures
    • DOI 10.1038/ncb1007-1110, PII NCB1007-1110
    • Chhabra ES, Higgs HN (2007). The many faces of actin: matching assembly factors with cellular structures. Nat Cell Biol 9, 1110-1121. (Pubitemid 47500485)
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 18
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosinfree, actin-rich compartment of the leading edge
    • DOI 10.1242/jcs.00147
    • DesMarais V, Ichetovkin I, Condeelis J, Hitchcock-DeGregori SE (2002). Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. J Cell Sci 115, 4649-4660. (Pubitemid 36007758)
    • (2002) Journal of Cell Science , vol.115 , Issue.23 , pp. 4649-4660
    • DesMarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-DeGregori, S.E.4
  • 19
    • 84871152095 scopus 로고    scopus 로고
    • Regulation of integrin trafficking, cell adhesion, and cell migration by WASH and the Arp2/3 complex
    • Duleh SN, Welch MD (2012). Regulation of integrin trafficking, cell adhesion, and cell migration by WASH and the Arp2/3 complex. Cytoskeleton (Hoboken) 69, 1047-1058.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 1047-1058
    • Duleh, S.N.1    Welch, M.D.2
  • 21
    • 84870520072 scopus 로고    scopus 로고
    • Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks
    • Gomez TS, Gorman JA, de Narvajas AA, Koenig AO, Billadeau DD (2012). Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks. Mol Biol Cell 23, 3215-3228.
    • (2012) Mol Biol Cell , vol.23 , pp. 3215-3228
    • Gomez, T.S.1    Gorman, J.A.2    De Narvajas, A.A.3    Koenig, A.O.4    Billadeau, D.D.5
  • 23
    • 84870209800 scopus 로고    scopus 로고
    • Rho family GTPases
    • Hall A (2012). Rho family GTPases. Biochem Soc Trans 40, 1378-1382.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1378-1382
    • Hall, A.1
  • 24
    • 12844269159 scopus 로고    scopus 로고
    • Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells
    • DOI 10.1091/mbc.E04-07-0555
    • Hotulainen P, Paunola E, Vartiainen MK, Lappalainen P (2005). Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol Biol Cell 16, 649-664. (Pubitemid 40165562)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.2 , pp. 649-664
    • Hotulainen, P.1    Paunola, E.2    Vartiainen, M.K.3    Lappalainen, P.4
  • 25
    • 0242558357 scopus 로고    scopus 로고
    • The verprolin-like central (vc) region of Wiskott-Aldrich syndrome protein induces Arp2/3 complex-dependent actin nucleation
    • Hufner K, Higgs HN, Pollard TD, Jacobi C, Aepfelbacher M, Linder S (2001). The verprolin-like central (vc) region of Wiskott-Aldrich syndrome protein induces Arp2/3 complex-dependent actin nucleation. J Biol Chem 276, 35761-35767.
    • (2001) J Biol Chem , vol.276 , pp. 35761-35767
    • Hufner, K.1    Higgs, H.N.2    Pollard, T.D.3    Jacobi, C.4    Aepfelbacher, M.5    Linder, S.6
  • 27
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • Iwasa JH, Mullins RD (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
  • 28
    • 33744514937 scopus 로고    scopus 로고
    • Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex
    • DOI 10.1074/jbc.M507470200
    • Kelly AE, Kranitz H, Dotsch V, Mullins RD (2006). Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex. J Biol Chem 281, 10589-10597. (Pubitemid 43864601)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10589-10597
    • Kelly, A.E.1    Kranitz, H.2    Dotsch, V.3    Mullins, R.D.4
  • 29
    • 40249118452 scopus 로고    scopus 로고
    • Differentially oriented populations of actin filaments generated in lamellipodia collaborate in pushing and pausing at the cell front
    • DOI 10.1038/ncb1692, PII NCB1692
    • Koestler SA, Auinger S, Vinzenz M, Rottner K, Small JV (2008). Differentially oriented populations of actin filaments generated in lamellipodia collaborate in pushing and pausing at the cell front. Nat Cell Biol 10, 306-313. (Pubitemid 351331017)
    • (2008) Nature Cell Biology , vol.10 , Issue.3 , pp. 306-313
    • Koestler, S.A.1    Auinger, S.2    Vinzenz, M.3    Rottner, K.4    Small, J.V.5
  • 30
    • 44349118518 scopus 로고    scopus 로고
    • Arp2/3 complex is important for filopodia formation, growth cone motility, and neuritogenesis in neuronal cells
    • DOI 10.1091/mbc.E07-09-0964
    • Korobova F, Svitkina T (2008). Arp2/3 complex is important for filopodia formation, growth cone motility, and neuritogenesis in neuronal cells. Mol Biol Cell 19, 1561-1574. (Pubitemid 351805109)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.4 , pp. 1561-1574
    • Korobova, F.1    Svitkina, T.2
  • 31
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • DOI 10.1006/jsbi.1996.0013
    • Kremer JR, Mastronarde DN, McIntosh JR (1996). Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116, 71-76. (Pubitemid 26093126)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 32
    • 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
    • DOI 10.1016/j.cub.2003.10.005
    • Kunda P, Craig G, Dominguez V, 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. (Pubitemid 37347929)
    • (2003) Current Biology , vol.13 , Issue.21 , pp. 1867-1875
    • Kunda, P.1    Craig, G.2    Dominguez, V.3    Baum, B.4
  • 34
    • 67749124073 scopus 로고    scopus 로고
    • Cortactin promotes migration and platelet-derived growth factor-induced actin reorganization by signaling to Rho-GTPases
    • Lai FP et al. (2009). Cortactin promotes migration and platelet-derived growth factor-induced actin reorganization by signaling to Rho-GTPases. Mol Biol Cell 20, 3209-3223.
    • (2009) Mol Biol Cell , vol.20 , pp. 3209-3223
    • Lai, F.P.1
  • 35
    • 0022653410 scopus 로고
    • The molecular organization of myosin in stress fibers of cultured cells
    • DOI 10.1083/jcb.102.1.200
    • Langanger G, Moeremans M, Daneels G, Sobieszek A, De Brabander M, De Mey J (1986). The molecular organization of myosin in stress fibers of cultured cells. J Cell Biol 102, 200-209. (Pubitemid 16155568)
    • (1986) Journal of Cell Biology , vol.102 , Issue.1 , pp. 200-209
    • Langanger, G.1    Moeremans, M.2    Daneels, G.3
  • 36
    • 70449112591 scopus 로고    scopus 로고
    • Activation of the WAVE complex by coincident signals controls actin assembly
    • Lebensohn AM, Kirschner MW (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
  • 37
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier MF (1999). Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401, 613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 38
    • 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
    • DOI 10.1093/embo-reports/kve197
    • Lommel S, Benesch S, Rottner K, Franz T, Wehland J, 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. (Pubitemid 32982755)
    • (2001) EMBO Reports , vol.2 , Issue.9 , pp. 850-857
    • Lommel, S.1    Benesch, S.2    Rottner, K.3    Franz, T.4    Wehland, J.5    Kuhn, R.6
  • 39
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky LM, Insall RH (1998). Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr Biol 8, 1347-1356. (Pubitemid 29020143)
    • (1998) Current Biology , vol.8 , Issue.25 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 40
    • 16244370745 scopus 로고    scopus 로고
    • Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death
    • DOI 10.1016/j.ejcb.2004.11.008, PII S0171933505000130
    • Mannherz HG, Gonsior SM, Gremm D, Wu X, Pope BJ, Weeds AG (2005). Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death. Eur J Cell Biol 84, 503-515. (Pubitemid 40450676)
    • (2005) European Journal of Cell Biology , vol.84 , Issue.4 , pp. 503-515
    • Mannherz, H.G.1    Gonsior, S.M.2    Gremm, D.3    Wu, X.4    Pope, B.J.5    Weeds, A.G.6
  • 41
    • 0035146636 scopus 로고    scopus 로고
    • Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
    • DOI 10.1038/35050590
    • Marchand JB, Kaiser DA, Pollard TD, Higgs HN (2001). Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. Nat Cell Biol 3, 76-82. (Pubitemid 32114835)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 76-82
    • Marchand, J.-B.1    Kaiser, D.A.2    Pollard, T.D.3    Higgs, H.N.4
  • 42
    • 0024421925 scopus 로고
    • Formation and movement of myosin-containing structures in living fibroblasts
    • McKenna NM, Wang YL, Konkel ME (1989). Formation and movement of myosin-containing structures in living fibroblasts. J Cell Biol 109, 1163-1172. (Pubitemid 19220098)
    • (1989) Journal of Cell Biology , vol.109 , Issue.3 , pp. 1163-1172
    • McKenna, N.M.1    Wang, Y.2    Konkel, M.E.3
  • 43
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: Pivotal role of the filament barbed end
    • DOI 10.1016/j.cell.2004.07.019, PII S0092867404007068
    • Mejillano MR, Kojima S, Applewhite DA, Gertler FB, Svitkina TM, Borisy GG (2004). Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118, 363-373. (Pubitemid 39061116)
    • (2004) Cell , vol.118 , Issue.3 , pp. 363-373
    • Mejillano, M.R.1    Kojima, S.-I.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5    Borisy, G.G.6
  • 44
    • 0037215933 scopus 로고    scopus 로고
    • Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5
    • DOI 10.1002/cm.10087
    • Millard TH, Behrendt B, Launay S, Futterer K, Machesky LM (2003). Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5. Cell Motil Cytoskeleton 54, 81-90. (Pubitemid 36033840)
    • (2003) Cell Motility and the Cytoskeleton , vol.54 , Issue.1 , pp. 81-90
    • Millard, T.H.1    Behrendt, B.2    Launay, S.3    Futterer, K.4    Machesky, L.M.5
  • 45
    • 84861410096 scopus 로고    scopus 로고
    • Diffusion, capture and recycling of SCAR/WAVE and Arp2/3 complexes observed in cells by single-molecule imaging
    • Millius A, Watanabe N, Weiner OD (2012). Diffusion, capture and recycling of SCAR/WAVE and Arp2/3 complexes observed in cells by single-molecule imaging. J Cell Sci 125, 1165-1176.
    • (2012) J Cell Sci , vol.125 , pp. 1165-1176
    • Millius, A.1    Watanabe, N.2    Weiner, O.D.3
  • 46
  • 48
    • 41549108457 scopus 로고    scopus 로고
    • Building the actin cytoskeleton: Filopodia contribute to the construction of contractile bundles in the lamella
    • DOI 10.1083/jcb.200709134
    • Nemethova M, Auinger S, Small JV (2008). Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella. J Cell Biol 180, 1233-1244. (Pubitemid 351468477)
    • (2008) Journal of Cell Biology , vol.180 , Issue.6 , pp. 1233-1244
    • Nemethova, M.1    Auinger, S.2    Small, J.V.3
  • 49
    • 55549116027 scopus 로고    scopus 로고
    • Arp2 depletion inhibits sheet-like protrusions but not linear protrusions of fibroblasts and lymphocytes
    • Nicholson-Dykstra SM, Higgs HN (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
  • 51
    • 79956109409 scopus 로고    scopus 로고
    • Microtubules as platforms for assaying actin polymerization in vivo
    • Oelkers JM et al. (2011). Microtubules as platforms for assaying actin polymerization in vivo. PLoS One 6, e19931.
    • (2011) PLoS One , vol.6
    • Oelkers, J.M.1
  • 52
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • DOI 10.1083/jcb.200110013
    • Ono S, Ono K (2002). Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J Cell Biol 156, 1065-1076. (Pubitemid 34839855)
    • (2002) Journal of Cell Biology , vol.156 , Issue.6 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 54
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • DOI 10.1016/S0092-8674(03)00120-X
    • Pollard TD, Borisy GG (2003). Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465. (Pubitemid 36263079)
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 55
    • 4544309783 scopus 로고    scopus 로고
    • Two distinct actin networks drive the protrusion of migrating cells
    • DOI 10.1126/science.1100533
    • Ponti A, Machacek M, Gupton SL, Waterman-Storer CM, Danuser G (2004). Two distinct actin networks drive the protrusion of migrating cells. Science 305, 1782-1786. (Pubitemid 39249647)
    • (2004) Science , vol.305 , Issue.5691 , pp. 1782-1786
    • Ponti, A.1    Machacek, M.2    Gupton, S.L.3    Waterman-Storer, C.M.4    Danuser, G.5
  • 56
    • 24944522416 scopus 로고    scopus 로고
    • Photobleaching techniques to study mobility and molecular dynamics of proteins in live cells: FRAP, iFRAP, and FLIP
    • ed RD Goldman and DL Spector, New York: Cold Spring Harbor Laboratory Press
    • Rabut G, Ellenberg J (2005). Photobleaching techniques to study mobility and molecular dynamics of proteins in live cells: FRAP, iFRAP, and FLIP. In: Live Cell Imaging, A Laboratory Manual, ed. RD Goldman and DL Spector, New York: Cold Spring Harbor Laboratory Press, 101-126.
    • (2005) Live Cell Imaging, A Laboratory Manual , pp. 101-126
    • Rabut, G.1    Ellenberg, J.2
  • 58
    • 79959677602 scopus 로고    scopus 로고
    • Life at the leading edge
    • Ridley AJ (2011). Life at the leading edge. Cell 145, 1012-1022.
    • (2011) Cell , vol.145 , pp. 1012-1022
    • Ridley, A.J.1
  • 60
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • DOI 10.1083/jcb.200303023
    • Rogers SL, Wiedemann U, Stuurman N, Vale RD (2003). Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J Cell Biol 162, 1079-1088. (Pubitemid 37174190)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 61
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • DOI 10.1016/S0960-9822(99)80286-3
    • Rottner K, Hall A, Small JV (1999). Interplay between Rac and Rho in the control of substrate contact dynamics. Curr Biol 9, 640-648. (Pubitemid 29291944)
    • (1999) Current Biology , vol.9 , Issue.12 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 62
    • 78049296901 scopus 로고    scopus 로고
    • WASH WHAMM and JMY: Regulation of Arp2/3 complex and beyond
    • Rottner K, Hanisch J, Campellone KG (2010). WASH, WHAMM and JMY: regulation of Arp2/3 complex and beyond. Trends Cell Biol 20, 650-661.
    • (2010) Trends Cell Biol , vol.20 , pp. 650-661
    • Rottner, K.1    Hanisch, J.2    Campellone, K.G.3
  • 63
    • 80053328974 scopus 로고    scopus 로고
    • Actin dynamics and turnover in cell motility
    • Rottner K, Stradal TE (2011). Actin dynamics and turnover in cell motility. Curr Opin Cell Biol 23, 569-578.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 569-578
    • Rottner, K.1    Stradal, T.E.2
  • 67
    • 0017802361 scopus 로고
    • Polarity of actin at the leading edge of cultured cells
    • DOI 10.1038/272638a0
    • Small JV, Isenberg G, Celis JE (1978). Polarity of actin at the leading edge of cultured cells. Nature 272, 638-639. (Pubitemid 8305197)
    • (1978) Nature , vol.272 , Issue.5654 , pp. 638-639
    • Small, J.V.1    Isenberg, G.2    Celis, J.E.3
  • 68
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: Coupling protrusion and retraction in cell motility
    • DOI 10.1016/j.ceb.2005.08.004, PII S0955067405001079
    • Small JV, Resch GP (2005). The comings and goings of actin: coupling protrusion and retraction in cell motility. Curr Opin Cell Biol 17, 517-523. (Pubitemid 41267166)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.5 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 69
    • 0036498546 scopus 로고    scopus 로고
    • The lamellipodium: Where motility begins
    • DOI 10.1016/S0962-8924(01)02237-1, PII S0962892401022371
    • Small JV, Stradal T, Vignal E, Rottner K (2002). The lamellipodium: where motility begins. Trends Cell Biol 12, 112-120. (Pubitemid 34164650)
    • (2002) Trends in Cell Biology , vol.12 , Issue.3 , pp. 112-120
    • Small J.Victor1    Stradal, T.2    Vignal, E.3    Rottner, K.4
  • 71
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S (1971). The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246, 4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 75
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni P, Rubinstein B, Unruh JR, Durnin M, Hanein D, 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
  • 76
    • 84882823562 scopus 로고    scopus 로고
    • Ultrastructure of protrusive actin filament arrays
    • Svitkina TM (2013). Ultrastructure of protrusive actin filament arrays. Curr Opin Cell Biol 25, 574-581.
    • (2013) Curr Opin Cell Biol , vol.25 , pp. 574-581
    • Svitkina, T.M.1
  • 77
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • DOI 10.1083/jcb.145.5.1009
    • Svitkina TM, Borisy GG (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. (Pubitemid 29270059)
    • (1999) Journal of Cell Biology , vol.145 , Issue.5 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 79
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: Mechanism of cell body translocation
    • DOI 10.1083/jcb.139.2.397
    • Svitkina TM, Verkhovsky AB, McQuade KM, Borisy GG (1997). Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J Cell Biol 139, 397-415. (Pubitemid 27459313)
    • (1997) Journal of Cell Biology , vol.139 , Issue.2 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 81
    • 77951977342 scopus 로고    scopus 로고
    • Electron tomography reveals unbranched networks of actin filaments in lamellipodia
    • Urban E, Jacob S, Nemethova M, Resch GP, Small JV (2010). Electron tomography reveals unbranched networks of actin filaments in lamellipodia. Nat Cell Biol 12, 429-435.
    • (2010) Nat Cell Biol , vol.12 , pp. 429-435
    • Urban, E.1    Jacob, S.2    Nemethova, M.3    Resch, G.P.4    Small, J.V.5
  • 82
    • 84866400870 scopus 로고    scopus 로고
    • SCAR knockouts in Dictyostelium: WASP assumes SCAR's position and upstream regulators in pseudopods
    • Veltman DM, King JS, Machesky LM, Insall RH (2012). SCAR knockouts in Dictyostelium: WASP assumes SCAR's position and upstream regulators in pseudopods. J Cell Biol 198, 501-508.
    • (2012) J Cell Biol , vol.198 , pp. 501-508
    • Veltman, D.M.1    King, J.S.2    Machesky, L.M.3    Insall, R.H.4
  • 83
    • 84859420307 scopus 로고    scopus 로고
    • Actin branching in the initiation and maintenance of lamellipodia
    • Vinzenz M et al. (2012). Actin branching in the initiation and maintenance of lamellipodia. J Cell Sci 125, 2775-2785.
    • (2012) J Cell Sci , vol.125 , pp. 2775-2785
    • Vinzenz, M.1
  • 84
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang YL (1985). Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol 101, 597-602.
    • (1985) J Cell Biol , vol.101 , pp. 597-602
    • Wang, Y.L.1
  • 85
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • DOI 10.1126/science.1067470
    • Watanabe N, Mitchison TJ (2002). Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295, 1083-1086. (Pubitemid 34132240)
    • (2002) Science , vol.295 , Issue.5557 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 86
    • 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 SA, Karginov AV, Schafer DA, Weaver AM, Kinley AW, Cooper JA, Parsons JT (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
  • 87
    • 61949147263 scopus 로고    scopus 로고
    • The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility
    • Weisswange I, Newsome TP, Schleich S, Way M (2009). The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. Nature 458, 87-91.
    • (2009) Nature , vol.458 , pp. 87-91
    • Weisswange, I.1    Newsome, T.P.2    Schleich, S.3    Way, M.4
  • 88
    • 84859426285 scopus 로고    scopus 로고
    • Actin filament tracking in electron tomograms of negatively stained lamellipodia using the localized radon transform
    • Winkler C, Vinzenz M, Small JV, Schmeiser C (2012). Actin filament tracking in electron tomograms of negatively stained lamellipodia using the localized radon transform. J Struct Biol 178, 19-28.
    • (2012) J Struct Biol , vol.178 , pp. 19-28
    • Winkler, C.1    Vinzenz, M.2    Small, J.V.3    Schmeiser, C.4
  • 90
    • 37249003725 scopus 로고    scopus 로고
    • Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells
    • Yang C, Czech L, Gerboth S, Kojima S, Scita G, Svitkina T (2007). Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells. PLoS Biol 5, e317.
    • (2007) PLoS Biol , vol.5
    • Yang, C.1    Czech, L.2    Gerboth, S.3    Kojima, S.4    Scita, G.5    Svitkina, T.6
  • 91
    • 84863734478 scopus 로고    scopus 로고
    • Arp2/3 complex-dependent actin networks constrain myosin II function in driving retrograde actin flow
    • Yang Q, Zhang XF, Pollard TD, Forscher P (2012). Arp2/3 complex-dependent actin networks constrain myosin II function in driving retrograde actin flow. J Cell Biol 197, 939-956.
    • (2012) J Cell Biol , vol.197 , pp. 939-956
    • Yang, Q.1    Zhang, X.F.2    Pollard, T.D.3    Forscher, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.