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Volumn 197, Issue 5, 2012, Pages 643-658

Stoichiometry of Nck-dependent actin polymerization in living cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; NCK PROTEIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 84862604526     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201111113     Document Type: Article
Times cited : (58)

References (64)
  • 1
    • 14044270698 scopus 로고    scopus 로고
    • In silico reconstitution of Listeria propulsion exhibits nano-saltation
    • Alberts, J.B., and G.M. Odell. 2004. In silico reconstitution of Listeria propulsion exhibits nano-saltation. PLoS Biol. 2:e412. http://dx.doi.org/10.1371/ journal.pbio.0020412
    • (2004) PLoS Biol , vol.2
    • Alberts, J.B.1    Odell, G.M.2
  • 2
    • 0032516877 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck
    • Antón, I.M., W. Lu, B.J. Mayer, N. Ramesh, and R.S. Geha. 1998. The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck. J. Biol. Chem. 273:20992-20995. http://dx.doi.org/ 10.1074/jbc.273.33.20992
    • (1998) J. Biol. Chem. , vol.273 , pp. 2099220995
    • Antón, I.M.1    Lu, W.2    Mayer, B.J.3    Ramesh, N.4    Geha, R.S.5
  • 3
    • 0036198683 scopus 로고    scopus 로고
    • WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation
    • Antón, I.M., M.A. de la Fuente, T.N. Sims, S. Freeman, N. Ramesh, J.H. Hartwig, M.L. Dustin, and R.S. Geha. 2002. WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation. Immunity. 16:193-204. http://dx.doi.org/10.1016/S1074-7613(02)00268-6
    • (2002) Immunity , vol.16 , pp. 193204
    • Antón, I.M.1    de la Fuente, M.A.2    Sims, T.N.3    Freeman, S.4    Ramesh, N.5    Hartwig, J.H.6    Dustin, M.L.7    Geha, R.S.8
  • 4
    • 12344272845 scopus 로고    scopus 로고
    • Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton
    • Barda-Saad, M., A. Braiman, R. Titerence, S.C. Bunnell, V.A. Barr, and L.E. Samelson. 2005. Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton. Nat. Immunol. 6:80-89. http:// dx.doi.org/10.1038/ni1143
    • (2005) Nat. Immunol. , vol.6 , pp. 8089
    • Barda-Saad, M.1    Braiman, A.2    Titerence, R.3    Bunnell, S.C.4    Barr, V.A.5    Samelson, L.E.6
  • 6
    • 43749107589 scopus 로고    scopus 로고
    • Pathway of actin filament branch formation by Arp2/3 complex
    • Beltzner C.C., and T.D. Pollard. 2008. Pathway of actin filament branch formation by Arp2/3 complex. J. Biol. Chem. 283:7135-7144. http://dx.doi.org/10.1074/jbc.M705894200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 71357144
    • Beltzner, C.C.1    Pollard, T.D.2
  • 7
    • 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., S. Lommel, A. Steffen, T.E. Stradal, N. Scaplehorn, M. Way, J. Wehland, and K. Rottner. 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. http://dx.doi.org/10.1074/jbc.M204145200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3777137776
    • 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
  • 8
    • 81155123707 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor 2 direct interaction with nephrin links VEGF-A signals to actin in kidney podocytes
    • Bertuccio C., D. Veron, P.K. Aggarwal, L. Holzman, and A. Tufro. 2011. Vascular endothelial growth factor receptor 2 direct interaction with nephrin links VEGF-A signals to actin in kidney podocytes. J. Biol. Chem. 286:39933-39944. http://dx.doi.org/10.1074/jbc.M111.241620.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3993339944
    • Bertuccio, C.1    Veron, D.2    Aggarwal, P.K.3    Holzman, L.4    Tufro, A.5
  • 9
  • 10
    • 0024759595 scopus 로고
    • Fluorescent cationic probes of mitochondria. Metrics and mechanism of interaction
    • Bunting, J.R., T.V. Phan, E. Kamali, and R.M. Dowben. 1989. Fluorescent cationic probes of mitochondria. Metrics and mechanism of interaction. Biophys. J. 56:979-993. http://dx.doi.org/10.1016/S0006-3495(89)82743-2.
    • (1989) Biophys. J. , vol.56 , pp. 979993
    • Bunting, J.R.1    Phan, T.V.2    Kamali, E.3    Dowben, R.M.4
  • 11
    • 0034698158 scopus 로고    scopus 로고
    • GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex
    • Carlier M.F., P. Nioche, I. Broutin-L'Hermite, R. Boujemaa, C. Le Clainche, C. Egile, C. Garbay, A. Ducruix, P. Sansonetti, and D. Pantaloni. 2000. GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex. J. Biol. Chem. 275:21946-21952. http://dx.doi.org/10.1074/jbc.M000687200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2194621952
    • Carlier, M.F.1    Nioche, P.2    Broutin-L'Hermite, I.3    Boujemaa, R.4    Le Clainche, C.5    Egile, C.6    Garbay, C.7    Ducruix, A.8    Sansonetti, P.9    Pantaloni, D.10
  • 12
    • 33646167587 scopus 로고    scopus 로고
    • Stimulation of actin polymerization by filament severing
    • Carlsson A.E. 2006. Stimulation of actin polymerization by filament severing. Biophys. J. 90:413-422. http://dx.doi.org/10.1529/biophysj.105.069765.
    • (2006) Biophys. J. , vol.90 , pp. 413422
    • Carlsson, A.E.1
  • 13
    • 1142310674 scopus 로고    scopus 로고
    • End versus side branching by Arp2/3 complex
    • Carlsson A.E., M.A. Wear, and J.A. Cooper. 2004. End versus side branching by Arp2/3 complex. Biophys. J. 86:1074-1081. http://dx.doi.org/ 10.1016/S0006-3495(04)74182-X
    • (2004) Biophys. J. , vol.86 , pp. 10741081
    • Carlsson, A.E.1    Wear, M.A.2    Cooper, J.A.3
  • 14
    • 67650391440 scopus 로고    scopus 로고
    • An open model of actin dendritic nucleation
    • Ditlev, J.A., N.M. Vacanti, I.L. Novak, and L.M. Loew. 2009. An open model of actin dendritic nucleation. Biophys. J. 96:3529-3542. http://dx.doi.org/10.1016/j.bpj.2009.01.037
    • (2009) Biophys. J. , vol.96 , pp. 35293542
    • Ditlev, J.A.1    Vacanti, N.M.2    Novak, I.L.3    Loew, L.M.4
  • 16
    • 0026767130 scopus 로고
    • Relative mitochondrial membrane potential and [Ca2+]i in type I cells isolated from the rabbit carotid body
    • Duchen, M.R., and T.J. Biscoe. 1992. Relative mitochondrial membrane potential and [Ca2+]i in type I cells isolated from the rabbit carotid body. J. Physiol. 450:33-61.
    • (1992) J. Physiol. , vol.450 , pp. 3361
    • Duchen, M.R.1    Biscoe, T.J.2
  • 17
    • 0031689215 scopus 로고    scopus 로고
    • Intracellular fluorescent probe concentrations by confocal microscopy
    • Fink, C., F. Morgan, and L.M. Loew. 1998. Intracellular fluorescent probe concentrations by confocal microscopy. Biophys. J. 75:1648-1658. http:// dx.doi.org/10.1016/S0006-3495(98)77607-6.
    • (1998) Biophys. J. , vol.75 , pp. 16481658
    • Fink, C.1    Morgan, F.2    Loew, L.M.3
  • 18
    • 0033613455 scopus 로고    scopus 로고
    • Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling
    • Frischknecht F., V. Moreau, S. Röttger, S. Gonfloni, I. Reckmann, G. Superti-Furga, and M. Way. 1999. Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Nature. 401:926-929. http://dx.doi.org/10.1038/44860.
    • (1999) Nature , vol.401 , pp. 926929
    • Frischknecht, F.1    Moreau, V.2    Röttger, S.3    Gonfloni, S.4    Reckmann, I.5    Superti-Furga, G.6    Way, M.7
  • 19
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42
    • Fukuoka M., S. Suetsugu, H. Miki, K. Fukami, T. Endo, and T. Takenawa. 2001. A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42. J. Cell Biol. 152:471-482. http://dx.doi.org/10.1083/jcb.152.3.471.
    • (2001) J. Cell Biol. , vol.152 , pp. 471482
    • Fukuoka, M.1    Suetsugu, S.2    Miki, H.3    Fukami, K.4    Endo, T.5    Takenawa, T.6
  • 20
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • Higgs H.N., and T.D. Pollard. 2000. Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150:1311-1320. http://dx.doi.org/10.1083/jcb.150.6.1311.
    • (2000) J. Cell Biol. , vol.150 , pp. 13111320
    • Higgs, H.N.1    Pollard, T.D.2
  • 24
    • 77955900382 scopus 로고    scopus 로고
    • Modeling capping protein FRAP and CALI experiments reveals in vivo regulation of actin dynamics
    • Kapustina, M., E. Vitriol, T.C. Elston, L.M. Loew, and K. Jacobson. 2010. Modeling capping protein FRAP and CALI experiments reveals in vivo regulation of actin dynamics. Cytoskeleton (Hoboken). 67:519-534.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 519-534
    • Kapustina, M.1    Vitriol, E.2    Elston, T.C.3    Loew, L.M.4    Jacobson, K.5
  • 25
    • 65649119024 scopus 로고    scopus 로고
    • Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion
    • Lapetina, S., C.C. Mader, K. Machida, B.J. Mayer, and A.J. Koleske. 2009. Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion. J. Cell Biol. 185:503-519. http://dx.doi.org/10.1083/jcb.200809085.
    • (2009) J. Cell Biol. , vol.185 , pp. 503519
    • Lapetina, S.1    Mader, C.C.2    Machida, K.3    Mayer, B.J.4    Koleske, A.J.5
  • 26
    • 33751229634 scopus 로고    scopus 로고
    • Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex
    • Mahaffy R.E., and T.D. Pollard. 2006. Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex. Biophys. J. 91:3519-3528. http://dx.doi.org/10.1529/biophysj.106.080937.
    • (2006) Biophys. J. , vol.91 , pp. 35193528
    • Mahaffy, R.E.1    Pollard, T.D.2
  • 27
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee J.D., and P.H. von Hippel. 1974. Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol. 86:469-489. http://dx.doi.org/10.1016/0022-2836(74)90031-X
    • (1974) J. Mol. Biol. , vol.86 , pp. 469489
    • McGhee, J.D.1    von Hippel, P.H.2
  • 28
    • 0242684547 scopus 로고    scopus 로고
    • The force-velocity relationship for the actin-based motility of Listeria monocytogenes
    • McGrath, J.L., N.J. Eungdamrong, C.I. Fisher, F. Peng, L. Mahadevan, T.J. Mitchison, and S.C. Kuo. 2003. The force-velocity relationship for the actin-based motility of Listeria monocytogenes. Curr. Biol. 13:329-332. http://dx.doi.org/10.1016/S0960-9822(03)00051-4.
    • (2003) Curr. Biol. , vol.13 , pp. 329332
    • McGrath, J.L.1    Eungdamrong, N.J.2    Fisher, C.I.3    Peng, F.4    Mahadevan, L.5    Mitchison, T.J.6    Kuo, S.C.7
  • 29
    • 77954124727 scopus 로고    scopus 로고
    • The effects of filament aging and annealing on a model lamellipodium undergoing disassembly by severing
    • Michalski P.J., and A.E. Carlsson. 2010. The effects of filament aging and annealing on a model lamellipodium undergoing disassembly by severing. Phys. Biol. 7:026004. http://dx.doi.org/10.1088/1478-3975/7/2/026004.
    • (2010) Phys. Biol. , vol.7 , pp. 026004
    • Michalski, P.J.1    Carlsson, A.E.2
  • 30
    • 30844458384 scopus 로고    scopus 로고
    • On the edge: Modeling protrusion
    • Mogilner A. 2006. On the edge: Modeling protrusion. Curr. Opin. Cell Biol. 18:32-39. http://dx.doi.org/10.1016/j.ceb.2005.11.001.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 3239
    • Mogilner, A.1
  • 31
    • 0033780474 scopus 로고    scopus 로고
    • A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
    • Moreau V., F. Frischknecht, I. Reckmann, R. Vincentelli, G. Rabut, D. Stewart, and M. Way. 2000. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat. Cell Biol. 2:441-448. http://dx.doi.org/10.1038/35017080.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 441448
    • Moreau, V.1    Frischknecht, F.2    Reckmann, I.3    Vincentelli, R.4    Rabut, G.5    Stewart, D.6    Way, M.7
  • 32
    • 50349095873 scopus 로고    scopus 로고
    • Quantitative analysis of G-actin transport in motile cells
    • Novak I.L., B.M. Slepchenko, and A. Mogilner. 2008. Quantitative analysis of G-actin transport in motile cells. Biophys. J. 95:1627-1638. http://dx.doi.org/10.1529/biophysj.108.130096.
    • (2008) Biophys. J. , vol.95 , pp. 16271638
    • Novak, I.L.1    Slepchenko, B.M.2    Mogilner, A.3
  • 33
    • 78149323428 scopus 로고    scopus 로고
    • Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia
    • Oser M., C.C. Mader, H. Gil-Henn, M. Magalhaes, J.J. Bravo-Cordero, A.J. Koleske, and J. Condeelis. 2010. Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia. J. Cell Sci. 123:3662-3673. http://dx.doi.org/10.1242/jcs.068163.
    • (2010) J. Cell Sci. , vol.123 , pp. 36623673
    • Oser, M.1    Mader, C.C.2    Gil-Henn, H.3    Magalhaes, M.4    Bravo-Cordero, J.J.5    Koleske, A.J.6    Condeelis, J.7
  • 34
    • 79151473957 scopus 로고    scopus 로고
    • Nck1 and Grb2 localization patterns can distinguish invadopodia from podosomes
    • Oser M., A. Dovas, D. Cox, and J. Condeelis. 2011. Nck1 and Grb2 localization patterns can distinguish invadopodia from podosomes. Eur. J. Cell Biol. 90:181-188. http://dx.doi.org/10.1016/j.ejcb.2010.08.006.
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 181188
    • Oser, M.1    Dovas, A.2    Cox, D.3    Condeelis, J.4
  • 35
    • 77953637330 scopus 로고    scopus 로고
    • Physical mechanisms of signal integration by WASP family proteins
    • Padrick S.B., and M.K. Rosen. 2010. Physical mechanisms of signal integration by WASP family proteins. Annu. Rev. Biochem. 79:707-735. http:// dx.doi.org/10.1146/annurev.biochem.77.060407.135452.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 707735
    • Padrick, S.B.1    Rosen, M.K.2
  • 38
    • 12344337525 scopus 로고    scopus 로고
    • A polybasic motif allows N-WASP to act as a sensor of PIP(2) density
    • Papayannopoulos V., C. Co, K.E. Prehoda, S. Snapper, J. Taunton, and W.A. Lim. 2005. A polybasic motif allows N-WASP to act as a sensor of PIP(2) density. Mol. Cell. 17:181-191. http://dx.doi.org/10.1016/j.molcel.2004.11.054.
    • (2005) Mol. Cell. , vol.17 , pp. 181191
    • Papayannopoulos, V.1    Co, C.2    Prehoda, K.E.3    Snapper, S.4    Taunton, J.5    Lim, W.A.6
  • 39
    • 80155136196 scopus 로고    scopus 로고
    • Studies of novel interactions between Nck and VAV SH3 domains
    • Pauker M.H., and M. Barda-Saad. 2011. Studies of novel interactions between Nck and VAV SH3 domains. Commun Integr Biol. 4:175-177. http:// dx.doi.org/10.4161/cib.4.2.14235.
    • (2011) Commun Integr Biol , vol.4 , pp. 175177
    • Pauker, M.H.1    Barda-Saad, M.2
  • 40
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson T. 2004. Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell. 116:191-203. http://dx.doi.org/10.1016/S0092-8674(03)01077-8.
    • (2004) Cell , vol.116 , pp. 191203
    • Pawson, T.1
  • 41
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard T.D. 2007. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36:451-477. http:// dx.doi.org/10.1146/annurev.biophys.35.040405.101936.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 451477
    • Pollard, T.D.1
  • 42
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and G.G. Borisy. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:453-465. http://dx.doi.org/10.1016/S0092-8674(03)00120-X
    • (2003) Cell , vol.112 , pp. 453465
    • Pollard, T.D.1    Borisy, G.G.2
  • 43
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda, K.E., J.A. Scott, R.D. Mullins, and W.A. Lim. 2000. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science. 290:801-806. http://dx.doi.org/10.1126/science.290.5492.801.
    • (2000) Science , vol.290 , pp. 801806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 44
    • 70350554308 scopus 로고    scopus 로고
    • Characterization of Wiskott-Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae
    • Rajmohan R., A. Raodah, M.H. Wong, and T. Thanabalu. 2009. Characterization of Wiskott-Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae. FEM. Yeast Res. 9:1226-1235. http://dx.doi.org/10.1111/ j.1567-1364.2009.00581.x
    • (2009) FEM. Yeast Res. , vol.9 , pp. 12261235
    • Rajmohan, R.1    Raodah, A.2    Wong, M.H.3    Thanabalu, T.4
  • 45
    • 33745478846 scopus 로고    scopus 로고
    • Dissecting Nck/Dock signaling pathways in Drosophila visual system
    • Rao, Y. 2005. Dissecting Nck/Dock signaling pathways in Drosophila visual system. Int. J. Biol. Sci. 1:80-86. http://dx.doi.org/10.7150/ijbs.1.80.
    • (2005) Int. J. Biol. Sci. , vol.1 , pp. 8086
    • Rao, Y.1
  • 46
    • 0032478083 scopus 로고    scopus 로고
    • Domain requirements for the Dock adapter protein in growth- cone signaling
    • Rao Y., and S.L. Zipursky. 1998. Domain requirements for the Dock adapter protein in growth- cone signaling. Proc. Natl. Acad. Sci. USA. 95:2077-2082. http://dx.doi.org/10.1073/pnas.95.5.2077.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 20772082
    • Rao, Y.1    Zipursky, S.L.2
  • 47
    • 0346965734 scopus 로고    scopus 로고
    • Inducible clustering of membrane-targeted SH3 domains of the adaptor protein Nck triggers localized actin polymerization
    • Rivera G.M., C.A. Briceño, F. Takeshima, S.B. Snapper, and B.J. Mayer. 2004. Inducible clustering of membrane-targeted SH3 domains of the adaptor protein Nck triggers localized actin polymerization. Curr. Biol. 14:11-22. http://dx.doi.org/10.1016/j.cub.2003.12.033.
    • (2004) Curr. Biol. , vol.14 , pp. 1122
    • Rivera, G.M.1    Briceño, C.A.2    Takeshima, F.3    Snapper, S.B.4    Mayer, B.J.5
  • 48
    • 33745447261 scopus 로고    scopus 로고
    • Requirement of Nck adaptors for actin dynamics and cell migration stimulated by platelet-derived growth factor B
    • Rivera G.M., S. Antoku, S. Gelkop, N.Y. Shin, S.K. Hanks, T. Pawson, and B.J. Mayer. 2006. Requirement of Nck adaptors for actin dynamics and cell migration stimulated by platelet-derived growth factor B. Proc. Natl. Acad. Sci. USA. 103:9536-9541. http://dx.doi.org/10.1073/ pnas.0603786103.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 95369541
    • Rivera, G.M.1    Antoku, S.2    Gelkop, S.3    Shin, N.Y.4    Hanks, S.K.5    Pawson, T.6    Mayer, B.J.7
  • 49
    • 70449130430 scopus 로고    scopus 로고
    • A reciprocal interdependence between Nck and PI(4,5)P(2) promotes localized N-WASp-mediated actin polymerization in living cells
    • Rivera G.M., D. Vasilescu, V. Papayannopoulos, W.A. Lim, and B.J. Mayer. 2009. A reciprocal interdependence between Nck and PI(4,5)P(2) promotes localized N-WASp-mediated actin polymerization in living cells. Mol. Cell. 36:525-535. http://dx.doi.org/10.1016/j.molcel.2009.10.025.
    • (2009) Mol. Cell. , vol.36 , pp. 525535
    • Rivera, G.M.1    Vasilescu, D.2    Papayannopoulos, V.3    Lim, W.A.4    Mayer, B.J.5
  • 50
    • 0035854732 scopus 로고    scopus 로고
    • Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi R., P. Nollau, H.Y. Ho, M.W. Kirschner, and B.J. Mayer. 2001. Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 276:26448-26452. http://dx.doi.org/10.1074/jbc.M103856200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2644826452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5
  • 51
    • 0033669220 scopus 로고    scopus 로고
    • Structural basis of Wiskott-Aldrich syndrome causing mutations in the WH1 domain
    • Rong S.B., and M. Vihinen. 2000. Structural basis of Wiskott-Aldrich syndrome causing mutations in the WH1 domain. J. Mol. Med. 78:530-537. http:// dx.doi.org/10.1007/s001090000136.
    • (2000) J. Mol. Med. , vol.78 , pp. 530537
    • Rong, S.B.1    Vihinen, M.2
  • 52
    • 50049123573 scopus 로고    scopus 로고
    • The pathogen protein EspF(U) hijacks actin polymerization using mimicry and multivalency
    • Sallee N.A., G.M. Rivera, J.E. Dueber, D. Vasilescu, R.D. Mullins, B.J. Mayer, and W.A. Lim. 2008. The pathogen protein EspF(U) hijacks actin polymerization using mimicry and multivalency. Nature. 454:1005-1008. http://dx.doi.org/10.1038/nature07170.
    • (2008) Nature , vol.454 , pp. 10051008
    • Sallee, N.A.1    Rivera, G.M.2    Dueber, J.E.3    Vasilescu, D.4    Mullins, R.D.5    Mayer, B.J.6    Lim, W.A.7
  • 53
    • 0036928182 scopus 로고    scopus 로고
    • Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation
    • Sasahara Y., R. Rachid, M.J. Byrne, M.A. de la Fuente, R.T. Abraham, N. Ramesh, and R.S. Geha. 2002. Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation. Mol. Cell. 10:1269-1281. http://dx.doi.org/10.1016/S1097-2765(02)00728-1.
    • (2002) Mol. Cell. , vol.10 , pp. 12691281
    • Sasahara, Y.1    Rachid, R.2    Byrne, M.J.3    de la Fuente, M.A.4    Abraham, R.T.5    Ramesh, N.6    Geha, R.S.7
  • 54
    • 0037197805 scopus 로고    scopus 로고
    • Grb2 and Nck act cooperatively to promote actinbased motility of vaccinia virus
    • Scaplehorn N., A. Holmström, V. Moreau, F. Frischknecht, I. Reckmann, and M. Way. 2002. Grb2 and Nck act cooperatively to promote actinbased motility of vaccinia virus. Curr. Biol. 12:740-745. http://dx.doi.org/10.1016/S0960-9822(02)00812-6.
    • (2002) Curr. Biol. , vol.12 , pp. 740745
    • Scaplehorn, N.1    Holmström, A.2    Moreau, V.3    Frischknecht, F.4    Reckmann, I.5    Way, M.6
  • 55
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • Sondermann P., R. Huber, V. Oosthuizen, and U. Jacob. 2000. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature. 406:267-273. http://dx.doi.org/10.1038/35018508
    • (2000) Nature , vol.406 , pp. 267273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 56
    • 0033561727 scopus 로고    scopus 로고
    • Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein
    • Stewart, D.M., L. Tian, and D.L. Nelson. 1999. Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein. J. Immunol. 162:5019-5024.
    • (1999) J. Immunol. , vol.162 , pp. 50195024
    • Stewart, D.M.1    Tian, L.2    Nelson, D.L.3
  • 57
    • 69549122682 scopus 로고    scopus 로고
    • Nck adaptor proteins link Tks5 to invadopodia actin regulation and ECM degradation
    • Stylli, S.S., T.T. Stacey, A.M. Verhagen, S.S. Xu, I. Pass, S.A. Courtneidge, and P. Lock. 2009. Nck adaptor proteins link Tks5 to invadopodia actin regulation and ECM degradation. J. Cell Sci. 122:2727-2740. http://dx.doi.org/10.1242/jcs.046680.
    • (2009) J. Cell Sci. , vol.122 , pp. 27272740
    • Stylli, S.S.1    Stacey, T.T.2    Verhagen, A.M.3    Xu, S.S.4    Pass, I.5    Courtneidge, S.A.6    Lock, P.7
  • 59
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
    • Ti S.C., C.T. Jurgenson, B.J. Nolen, and T.D. Pollard. 2011. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc. Natl. Acad. Sci. USA. 108: E463-E471. http://dx.doi.org/10.1073/pnas.1100125108.
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108
    • Ti, S.C.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 60
    • 33646401549 scopus 로고    scopus 로고
    • Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization
    • Verma R., I. Kovari, A. Soofi, D. Nihalani, K. Patrie, and L.B. Holzman. 2006. Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization. J. Clin. Invest. 116:1346-1359. http://dx.doi.org/10.1172/JCI27414.
    • (2006) J. Clin. Invest. , vol.116 , pp. 13461359
    • Verma, R.1    Kovari, I.2    Soofi, A.3    Nihalani, D.4    Patrie, K.5    Holzman, L.B.6
  • 61
    • 61949147263 scopus 로고    scopus 로고
    • The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility
    • Weisswange I., T.P. Newsome, S. Schleich, and M. Way. 2009. The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. Nature. 458:87-91. http://dx.doi.org/10.1038/nature07773.
    • (2009) Nature , vol.458 , pp. 8791
    • Weisswange, I.1    Newsome, T.P.2    Schleich, S.3    Way, M.4
  • 62
    • 0037415575 scopus 로고    scopus 로고
    • A biomimetic motility assay provides insight into the mechanism of actin-based motility
    • Wiesner S., E. Helfer, D. Didry, G. Ducouret, F. Lafuma, M.F. Carlier, and D. Pantaloni. 2003. A biomimetic motility assay provides insight into the mechanism of actin-based motility. J. Cell Biol. 160:387-398. http:// dx.doi.org/10.1083/jcb.200207148.
    • (2003) J. Cell Biol. , vol.160 , pp. 387398
    • Wiesner, S.1    Helfer, E.2    Didry, D.3    Ducouret, G.4    Lafuma, F.5    Carlier, M.F.6    Pantaloni, D.7
  • 63
    • 26844562643 scopus 로고    scopus 로고
    • Counting cytokinesis proteins globally and locally in fission yeast
    • Wu J.Q., and T.D. Pollard. 2005. Counting cytokinesis proteins globally and locally in fission yeast. Science. 310:310-314. http://dx.doi.org/10.1126/ science.1113230.
    • (2005) Science , vol.310 , pp. 310314
    • Wu, J.Q.1    Pollard, T.D.2


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