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Volumn 24, Issue 4, 2013, Pages 308-313

WASPs and WAVEs: From molecular function to physiology in hematopoietic cells

Author keywords

Arp2 3 complex; Endocytosis; Enteropathogenic and enterohaemorrhagic Escherichia coli; Lemellipodia; Nucleation promoting factor; Podosome; Pseudopod

Indexed keywords

MEMBRANE PROTEIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PROLINE; UNCLASSIFIED DRUG; WAVE PROTEIN;

EID: 84876729412     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2013.03.002     Document Type: Review
Times cited : (9)

References (83)
  • 1
  • 2
    • 70450245305 scopus 로고    scopus 로고
    • Actin filament nucleation and elongation factors-structure-function relationships
    • Dominguez R. Actin filament nucleation and elongation factors-structure-function relationships. Critical Reviews in Biochemistry and Molecular Biology 2009, 44:351-366.
    • (2009) Critical Reviews in Biochemistry and Molecular Biology , vol.44 , pp. 351-366
    • Dominguez, R.1
  • 4
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
    • Takenawa T., Suetsugu S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nature Reviews Molecular Cell Biology 2007, 8:37-48.
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 5
    • 69549114949 scopus 로고    scopus 로고
    • WASP and SCAR/WAVE proteins: the drivers of actin assembly
    • Pollitt A.Y., Insall R.H. WASP and SCAR/WAVE proteins: the drivers of actin assembly. Journal of Cell Science 2009, 122:2575-2578.
    • (2009) Journal of Cell Science , vol.122 , pp. 2575-2578
    • Pollitt, A.Y.1    Insall, R.H.2
  • 6
    • 77957039464 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: friends or foes in cancer invasion
    • Kurisu S., Takenawa T. WASP and WAVE family proteins: friends or foes in cancer invasion. Cancer Science 2010, 101:2093-2104.
    • (2010) Cancer Science , vol.101 , pp. 2093-2104
    • Kurisu, S.1    Takenawa, T.2
  • 8
    • 84858136256 scopus 로고    scopus 로고
    • Evolution of the eukaryotic ARP2/3 activators of the WASP family: WASP, WAVE, WASH, and WHAMM, and the proposed new family members WAWH and WAML
    • Kollmar M., Lbik D., Enge S. Evolution of the eukaryotic ARP2/3 activators of the WASP family: WASP, WAVE, WASH, and WHAMM, and the proposed new family members WAWH and WAML. BMC Research Notes 2012, 5:88.
    • (2012) BMC Research Notes , vol.5 , pp. 88
    • Kollmar, M.1    Lbik, D.2    Enge, S.3
  • 9
    • 69849096613 scopus 로고    scopus 로고
    • Mutations of the Wiskott-Aldrich syndrome protein affect protein expression and dictate the clinical phenotypes
    • Ochs H.D. Mutations of the Wiskott-Aldrich syndrome protein affect protein expression and dictate the clinical phenotypes. Immunologic Research 2009, 44:84-88.
    • (2009) Immunologic Research , vol.44 , pp. 84-88
    • Ochs, H.D.1
  • 12
    • 69849084692 scopus 로고    scopus 로고
    • Recent advances in the biology of WASP and WIP
    • Ramesh N., Geha R. Recent advances in the biology of WASP and WIP. Immunologic Research 2009, 44:99-111.
    • (2009) Immunologic Research , vol.44 , pp. 99-111
    • Ramesh, N.1    Geha, R.2
  • 14
    • 33846260575 scopus 로고    scopus 로고
    • WIP null mice display a progressive immunological disorder that resembles Wiskott-Aldrich syndrome
    • Curcio C., Pannellini T., Lanzardo S., Forni G., Musiani P., Anton I.M. WIP null mice display a progressive immunological disorder that resembles Wiskott-Aldrich syndrome. Journal of Pathology 2007, 211:67-75.
    • (2007) Journal of Pathology , vol.211 , pp. 67-75
    • Curcio, C.1    Pannellini, T.2    Lanzardo, S.3    Forni, G.4    Musiani, P.5    Anton, I.M.6
  • 15
    • 40549089536 scopus 로고    scopus 로고
    • Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation
    • Ayala I., Baldassarre M., Giacchetti G., Caldieri G., Tete S., Luini A., et al. Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation. Journal of Cell Science 2008, 121:369-378.
    • (2008) Journal of Cell Science , vol.121 , pp. 369-378
    • Ayala, I.1    Baldassarre, M.2    Giacchetti, G.3    Caldieri, G.4    Tete, S.5    Luini, A.6
  • 16
    • 33745482350 scopus 로고    scopus 로고
    • Inhibition of calpain stabilises podosomes and impairs dendritic cell motility
    • Calle Y., Carragher N.O., Thrasher A.J., Jones G.E. Inhibition of calpain stabilises podosomes and impairs dendritic cell motility. Journal of Cell Science 2006, 119:2375-2385.
    • (2006) Journal of Cell Science , vol.119 , pp. 2375-2385
    • Calle, Y.1    Carragher, N.O.2    Thrasher, A.J.3    Jones, G.E.4
  • 17
    • 0032530670 scopus 로고    scopus 로고
    • Collagen induces tyrosine phosphorylation of Wiskott-Aldrich syndrome protein in human platelets
    • Oda A., Ochs H.D., Druker B.J., Ozaki K., Watanabe C., Handa M., et al. Collagen induces tyrosine phosphorylation of Wiskott-Aldrich syndrome protein in human platelets. Blood 1998, 92:1852-1858.
    • (1998) Blood , vol.92 , pp. 1852-1858
    • Oda, A.1    Ochs, H.D.2    Druker, B.J.3    Ozaki, K.4    Watanabe, C.5    Handa, M.6
  • 19
    • 0032403083 scopus 로고    scopus 로고
    • WAVE a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki H., Suetsugu S., Takenawa T. WAVE a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO Journal 1998, 17:6932-6941.
    • (1998) EMBO Journal , vol.17 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 20
    • 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., Insall R.H. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Current Biology 1998, 8:1347-1356.
    • (1998) Current Biology , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 22
    • 46149096223 scopus 로고    scopus 로고
    • WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport
    • Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D. WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 2008, 134:148-161.
    • (2008) Cell , vol.134 , pp. 148-161
    • Campellone, K.G.1    Webb, N.J.2    Znameroski, E.A.3    Welch, M.D.4
  • 24
    • 78049296901 scopus 로고    scopus 로고
    • WASH, WHAMM and JMY: regulation of Arp2/3 complex and beyond
    • Rottner K., Hanisch J., Campellone K.G. WASH, WHAMM and JMY: regulation of Arp2/3 complex and beyond. Trends in Cell Biology 2010, 20:650-661.
    • (2010) Trends in Cell Biology , vol.20 , pp. 650-661
    • Rottner, K.1    Hanisch, J.2    Campellone, K.G.3
  • 25
    • 50049086091 scopus 로고    scopus 로고
    • Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U)
    • Cheng H.C., Skehan B.M., Campellone K.G., Leong J.M., Rosen M.K. Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U). Nature 2008, 454:1009-1013.
    • (2008) Nature , vol.454 , pp. 1009-1013
    • Cheng, H.C.1    Skehan, B.M.2    Campellone, K.G.3    Leong, J.M.4    Rosen, M.K.5
  • 26
    • 77958128363 scopus 로고    scopus 로고
    • Enterohemorrhagic E. coli requires N-WASP for efficient type III translocation but not for EspFU-mediated actin pedestal formation
    • Vingadassalom D., Campellone K.G., Brady M.J., Skehan B., Battle S.E., Robbins D., et al. Enterohemorrhagic E. coli requires N-WASP for efficient type III translocation but not for EspFU-mediated actin pedestal formation. PLoS Pathogens 2010, 6:e1001056.
    • (2010) PLoS Pathogens , vol.6
    • Vingadassalom, D.1    Campellone, K.G.2    Brady, M.J.3    Skehan, B.4    Battle, S.E.5    Robbins, D.6
  • 27
    • 0035964794 scopus 로고    scopus 로고
    • Structure of Arp2/3 complex in its activated state and in actin filament branch junctions
    • Volkmann N., Amann K.J., Stoilova-McPhie S., Egile C., Winter D.C., Hazelwood L., et al. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 2001, 293:2456-2459.
    • (2001) Science , vol.293 , pp. 2456-2459
    • Volkmann, N.1    Amann, K.J.2    Stoilova-McPhie, S.3    Egile, C.4    Winter, D.C.5    Hazelwood, L.6
  • 28
    • 84855359693 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors
    • Xu X.P., Rouiller I., Slaughter B.D., Egile C., Kim E., Unruh J.R., et al. Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors. EMBO Journal 2012, 31:236-247.
    • (2012) EMBO Journal , vol.31 , pp. 236-247
    • Xu, X.P.1    Rouiller, I.2    Slaughter, B.D.3    Egile, C.4    Kim, E.5    Unruh, J.R.6
  • 29
    • 0037112347 scopus 로고    scopus 로고
    • Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich syndrome
    • Volkman B.F., Prehoda K.E., Scott J.A., Peterson F.C., Lim W.A. Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich syndrome. Cell 2002, 111:565-576.
    • (2002) Cell , vol.111 , pp. 565-576
    • Volkman, B.F.1    Prehoda, K.E.2    Scott, J.A.3    Peterson, F.C.4    Lim, W.A.5
  • 30
    • 79960734724 scopus 로고    scopus 로고
    • Identification of Fyn as the binding partner for the WASP N-terminal domain in T cells
    • Sato M., Sawahata R., Takenouchi T., Kitani H. Identification of Fyn as the binding partner for the WASP N-terminal domain in T cells. International Immunology 2011, 23:493-502.
    • (2011) International Immunology , vol.23 , pp. 493-502
    • Sato, M.1    Sawahata, R.2    Takenouchi, T.3    Kitani, H.4
  • 31
    • 84855813364 scopus 로고    scopus 로고
    • Critical roles of the WASP N-terminal domain and Btk in LPS-induced inflammatory response in macrophages
    • Sakuma C., Sato M., Takenouchi T., Chiba J., Kitani H. Critical roles of the WASP N-terminal domain and Btk in LPS-induced inflammatory response in macrophages. PLoS ONE 2012, 7:e30351.
    • (2012) PLoS ONE , vol.7
    • Sakuma, C.1    Sato, M.2    Takenouchi, T.3    Chiba, J.4    Kitani, H.5
  • 34
    • 79959314184 scopus 로고    scopus 로고
    • High-resolution X-ray structure of the trimeric Scar/WAVE-complex precursor Brk1
    • Linkner J., Witte G., Stradal T., Curth U., Faix J. High-resolution X-ray structure of the trimeric Scar/WAVE-complex precursor Brk1. PLoS ONE 2011, 6:e21327.
    • (2011) PLoS ONE , vol.6
    • Linkner, J.1    Witte, G.2    Stradal, T.3    Curth, U.4    Faix, J.5
  • 35
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki H., Miura K., Takenawa T. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO Journal 1996, 15:5326-5335.
    • (1996) EMBO Journal , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 36
    • 3242669146 scopus 로고    scopus 로고
    • Regulation of WASP: PIP2 Pipped by Toca-1
    • Insall R.H., Machesky L.M. Regulation of WASP: PIP2 Pipped by Toca-1. Cell 2004, 118:140-141.
    • (2004) Cell , vol.118 , pp. 140-141
    • Insall, R.H.1    Machesky, L.M.2
  • 37
    • 33947382640 scopus 로고    scopus 로고
    • Differential regulation of WASP and N-WASP by Cdc42, Rac1, Nck, and PI(4,5)P2
    • Tomasevic N., Jia Z., Russell A., Fujii T., Hartman J.J., Clancy S., et al. Differential regulation of WASP and N-WASP by Cdc42, Rac1, Nck, and PI(4,5)P2. Biochemistry 2007, 46:3494-3502.
    • (2007) Biochemistry , vol.46 , pp. 3494-3502
    • Tomasevic, N.1    Jia, Z.2    Russell, A.3    Fujii, T.4    Hartman, J.J.5    Clancy, S.6
  • 38
    • 71349086233 scopus 로고    scopus 로고
    • Directional control of WAVE2 membrane targeting by EB1 and phosphatidylinositol 3,4,5-triphosphate
    • Takahashi K., Tanaka T., Suzuki K. Directional control of WAVE2 membrane targeting by EB1 and phosphatidylinositol 3,4,5-triphosphate. Cellular Signalling 2010, 22:510-518.
    • (2010) Cellular Signalling , vol.22 , pp. 510-518
    • Takahashi, K.1    Tanaka, T.2    Suzuki, K.3
  • 40
    • 79959541003 scopus 로고    scopus 로고
    • The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function
    • Murphy D.A., Courtneidge S.A. The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nature Reviews Molecular Cell Biology 2011, 12:413-426.
    • (2011) Nature Reviews Molecular Cell Biology , vol.12 , pp. 413-426
    • Murphy, D.A.1    Courtneidge, S.A.2
  • 42
    • 79959677602 scopus 로고    scopus 로고
    • Life at the leading edge
    • Ridley A.J. Life at the leading edge. Cell 2011, 145:1012-1022.
    • (2011) Cell , vol.145 , pp. 1012-1022
    • Ridley, A.J.1
  • 44
    • 84867399470 scopus 로고    scopus 로고
    • Pathological roles of invadopodia in cancer invasion and metastasis
    • Yamaguchi H. Pathological roles of invadopodia in cancer invasion and metastasis. European Journal of Cell Biology 2012.
    • (2012) European Journal of Cell Biology
    • Yamaguchi, H.1
  • 46
    • 66749105083 scopus 로고    scopus 로고
    • PtdIns(3,4)P2 instigates focal adhesions to generate podosomes
    • Oikawa T., Takenawa T. PtdIns(3,4)P2 instigates focal adhesions to generate podosomes. Cell Adhesion and Migration 2009, 3:195-197.
    • (2009) Cell Adhesion and Migration , vol.3 , pp. 195-197
    • Oikawa, T.1    Takenawa, T.2
  • 47
    • 0034842129 scopus 로고    scopus 로고
    • Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells
    • Gruenheid S., DeVinney R., Bladt F., Goosney D., Gelkop S., Gish G.D., et al. Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells. Nature Cell Biology 2001, 3:856-859.
    • (2001) Nature Cell Biology , vol.3 , pp. 856-859
    • Gruenheid, S.1    DeVinney, R.2    Bladt, F.3    Goosney, D.4    Gelkop, S.5    Gish, G.D.6
  • 48
    • 33748964289 scopus 로고    scopus 로고
    • Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis
    • Dawson J.C., Legg J.A., Machesky L.M. Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis. Trends in Cell Biology 2006, 16:493-498.
    • (2006) Trends in Cell Biology , vol.16 , pp. 493-498
    • Dawson, J.C.1    Legg, J.A.2    Machesky, L.M.3
  • 51
    • 77957916873 scopus 로고    scopus 로고
    • Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: implications for endocytosis
    • Bu W., Lim K.B., Yu Y.H., Chou A.M., Sudhaharan T., Ahmed S. Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: implications for endocytosis. PLoS ONE 2010, 5:e12153.
    • (2010) PLoS ONE , vol.5
    • Bu, W.1    Lim, K.B.2    Yu, Y.H.3    Chou, A.M.4    Sudhaharan, T.5    Ahmed, S.6
  • 53
    • 0141886295 scopus 로고    scopus 로고
    • Differential roles of WAVE1 and WAVE2 in dorsal and peripheral ruffle formation for fibroblast cell migration
    • Suetsugu S., Yamazaki D., Kurisu S., Takenawa T. Differential roles of WAVE1 and WAVE2 in dorsal and peripheral ruffle formation for fibroblast cell migration. Developmental Cell 2003, 5:595-609.
    • (2003) Developmental Cell , vol.5 , pp. 595-609
    • Suetsugu, S.1    Yamazaki, D.2    Kurisu, S.3    Takenawa, T.4
  • 54
    • 36348957943 scopus 로고    scopus 로고
    • The WAVE2/Abi1 complex differentially regulates megakaryocyte development and spreading: implications for platelet biogenesis and spreading machinery
    • Eto K., Nishikii H., Ogaeri T., Suetsugu S., Kamiya A., Kobayashi T., et al. The WAVE2/Abi1 complex differentially regulates megakaryocyte development and spreading: implications for platelet biogenesis and spreading machinery. Blood 2007, 110:3637-3647.
    • (2007) Blood , vol.110 , pp. 3637-3647
    • Eto, K.1    Nishikii, H.2    Ogaeri, T.3    Suetsugu, S.4    Kamiya, A.5    Kobayashi, T.6
  • 55
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac
    • Suetsugu S., Kurisu S., Oikawa T., Yamazaki D., Oda A., Takenawa T. Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac. Journal of Cell Biology 2006, 173:571-585.
    • (2006) Journal of Cell Biology , vol.173 , pp. 571-585
    • Suetsugu, S.1    Kurisu, S.2    Oikawa, T.3    Yamazaki, D.4    Oda, A.5    Takenawa, T.6
  • 56
    • 84856945929 scopus 로고    scopus 로고
    • MDia1 and WAVE2 proteins interact directly with IRSp53 in filopodia and are involved in filopodium formation
    • Goh W.I., Lim K.B., Sudhaharan T., Sem K.P., Bu W., Chou A.M., et al. mDia1 and WAVE2 proteins interact directly with IRSp53 in filopodia and are involved in filopodium formation. Journal of Biological Chemistry 2012, 287:4702-4714.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 4702-4714
    • Goh, W.I.1    Lim, K.B.2    Sudhaharan, T.3    Sem, K.P.4    Bu, W.5    Chou, A.M.6
  • 57
    • 84858665656 scopus 로고    scopus 로고
    • The adaptor molecule Nck localizes the WAVE complex to promote actin polymerization during CEACAM3-mediated phagocytosis of bacteria
    • Pils S., Kopp K., Peterson L., Delgado Tascon J., Nyffenegger-Jann N.J., Hauck C.R. The adaptor molecule Nck localizes the WAVE complex to promote actin polymerization during CEACAM3-mediated phagocytosis of bacteria. PLoS ONE 2012, 7:e32808.
    • (2012) PLoS ONE , vol.7
    • Pils, S.1    Kopp, K.2    Peterson, L.3    Delgado Tascon, J.4    Nyffenegger-Jann, N.J.5    Hauck, C.R.6
  • 58
    • 0032422123 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42
    • Guinamard R., Aspenstrom P., Fougereau M., Chavrier P., Guillemot J.C. Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42. FEBS Letters 1998, 434:431-436.
    • (1998) FEBS Letters , vol.434 , pp. 431-436
    • Guinamard, R.1    Aspenstrom, P.2    Fougereau, M.3    Chavrier, P.4    Guillemot, J.C.5
  • 59
    • 0036850180 scopus 로고    scopus 로고
    • Sustained activation of N-WASP through phosphorylation is essential for neurite extension
    • Suetsugu S., Hattori M., Miki H., Tezuka T., Yamamoto T., Mikoshiba K., et al. Sustained activation of N-WASP through phosphorylation is essential for neurite extension. Developmental Cell 2002, 3:645-658.
    • (2002) Developmental Cell , vol.3 , pp. 645-658
    • Suetsugu, S.1    Hattori, M.2    Miki, H.3    Tezuka, T.4    Yamamoto, T.5    Mikoshiba, K.6
  • 60
    • 38349018449 scopus 로고    scopus 로고
    • Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity
    • Danson C.M., Pocha S.M., Bloomberg G.B., Cory G.O. Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity. Journal of Cell Science 2007, 120:4144-4154.
    • (2007) Journal of Cell Science , vol.120 , pp. 4144-4154
    • Danson, C.M.1    Pocha, S.M.2    Bloomberg, G.B.3    Cory, G.O.4
  • 61
    • 33845986367 scopus 로고    scopus 로고
    • C-Abl interacts with the WAVE2 signaling complex to induce membrane ruffling and cell spreading
    • Stuart J.R., Gonzalez F.H., Kawai H., Yuan Z.M. c-Abl interacts with the WAVE2 signaling complex to induce membrane ruffling and cell spreading. Journal of Biological Chemistry 2006, 281:31290-31297.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 31290-31297
    • Stuart, J.R.1    Gonzalez, F.H.2    Kawai, H.3    Yuan, Z.M.4
  • 62
    • 58149333848 scopus 로고    scopus 로고
    • WAVE2 is regulated by multiple phosphorylation events within its VCA domain
    • Pocha S.M., Cory G.O. WAVE2 is regulated by multiple phosphorylation events within its VCA domain. Cell Motility and the Cytoskeleton 2009, 66:36-47.
    • (2009) Cell Motility and the Cytoskeleton , vol.66 , pp. 36-47
    • Pocha, S.M.1    Cory, G.O.2
  • 63
    • 51149123070 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of WAVE2 regulates oligodendrocyte precursor cell migration through nonreceptor tyrosine kinase Fyn
    • Miyamoto Y., Yamauchi J., Tanoue A. Cdk5 phosphorylation of WAVE2 regulates oligodendrocyte precursor cell migration through nonreceptor tyrosine kinase Fyn. Journal of Neuroscience 2008, 28:8326-8337.
    • (2008) Journal of Neuroscience , vol.28 , pp. 8326-8337
    • Miyamoto, Y.1    Yamauchi, J.2    Tanoue, A.3
  • 64
    • 33747482904 scopus 로고    scopus 로고
    • Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology
    • Kim Y., Sung J.Y., Ceglia I., Lee K.W., Ahn J.H., Halford J.M., et al. Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology. Nature 2006, 442:814-817.
    • (2006) Nature , vol.442 , pp. 814-817
    • Kim, Y.1    Sung, J.Y.2    Ceglia, I.3    Lee, K.W.4    Ahn, J.H.5    Halford, J.M.6
  • 65
    • 33645771745 scopus 로고    scopus 로고
    • Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin
    • Mitsushima M., Sezaki T., Akahane R., Ueda K., Suetsugu S., Takenawa T., et al. Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin. Genes to Cells 2006, 11:281-292.
    • (2006) Genes to Cells , vol.11 , pp. 281-292
    • Mitsushima, M.1    Sezaki, T.2    Akahane, R.3    Ueda, K.4    Suetsugu, S.5    Takenawa, T.6
  • 66
    • 0043267980 scopus 로고    scopus 로고
    • WAVE2 is required for directed cell migration and cardiovascular development
    • Yamazaki D., Suetsugu S., Miki H., Kataoka Y., Nishikawa S., Fujiwara T., et al. WAVE2 is required for directed cell migration and cardiovascular development. Nature 2003, 424:452-456.
    • (2003) Nature , vol.424 , pp. 452-456
    • Yamazaki, D.1    Suetsugu, S.2    Miki, H.3    Kataoka, Y.4    Nishikawa, S.5    Fujiwara, T.6
  • 68
    • 84866400870 scopus 로고    scopus 로고
    • SCAR knockouts in Dictyostelium: WASP assumes SCAR's position and upstream regulators in pseudopods
    • Veltman D.M., King J.S., Machesky L.M., Insall R.H. SCAR knockouts in Dictyostelium: WASP assumes SCAR's position and upstream regulators in pseudopods. Journal of Cell Biology 2012, 198:501-508.
    • (2012) Journal of Cell Biology , vol.198 , pp. 501-508
    • Veltman, D.M.1    King, J.S.2    Machesky, L.M.3    Insall, R.H.4
  • 69
    • 77956537388 scopus 로고    scopus 로고
    • Self-assembly of filopodia-like structures on supported lipid bilayers
    • Lee K., Gallop J.L., Rambani K., Kirschner M.W. Self-assembly of filopodia-like structures on supported lipid bilayers. Science 2010, 329:1341-1345.
    • (2010) Science , vol.329 , pp. 1341-1345
    • Lee, K.1    Gallop, J.L.2    Rambani, K.3    Kirschner, M.W.4
  • 70
    • 0034501036 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein and platelets
    • Oda A., Ochs H.D. Wiskott-Aldrich syndrome protein and platelets. Immunological Reviews 2000, 178:111-117.
    • (2000) Immunological Reviews , vol.178 , pp. 111-117
    • Oda, A.1    Ochs, H.D.2
  • 71
    • 84862917711 scopus 로고    scopus 로고
    • The chemotactic defect in Wiskott-Aldrich syndrome macrophages is due to the reduced persistence of directional protrusions
    • Ishihara D., Dovas A., Park H., Isaac B.M., Cox D. The chemotactic defect in Wiskott-Aldrich syndrome macrophages is due to the reduced persistence of directional protrusions. PLoS ONE 2012, 7:e30033.
    • (2012) PLoS ONE , vol.7
    • Ishihara, D.1    Dovas, A.2    Park, H.3    Isaac, B.M.4    Cox, D.5
  • 73
    • 78149413594 scopus 로고    scopus 로고
    • N-WASP has the ability to compensate for the loss of WASP in macrophage podosome formation and chemotaxis
    • Isaac B.M., Ishihara D., Nusblat L.M., Gevrey J.C., Dovas A., Condeelis J., et al. N-WASP has the ability to compensate for the loss of WASP in macrophage podosome formation and chemotaxis. Experimental Cell Research 2010, 316:3406-3416.
    • (2010) Experimental Cell Research , vol.316 , pp. 3406-3416
    • Isaac, B.M.1    Ishihara, D.2    Nusblat, L.M.3    Gevrey, J.C.4    Dovas, A.5    Condeelis, J.6
  • 74
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi H., Condeelis J. Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochimica et Biophysica Acta 2007, 1773:642-652.
    • (2007) Biochimica et Biophysica Acta , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 77
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: linking membrane trafficking with the cytoskeleton
    • Kessels M.M., Qualmann B. The syndapin protein family: linking membrane trafficking with the cytoskeleton. Journal of Cell Science 2004, 117:3077-3086.
    • (2004) Journal of Cell Science , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 78
    • 33748994545 scopus 로고    scopus 로고
    • GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Rho Ridley A.J. GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends in Cell Biology 2006, 16:522-529.
    • (2006) Trends in Cell Biology , vol.16 , pp. 522-529
    • Rho, R.A.J.1
  • 79
    • 77956454496 scopus 로고    scopus 로고
    • Cdc42 and vesicle trafficking in polarized cells
    • Harris K.P., Tepass U. Cdc42 and vesicle trafficking in polarized cells. Traffic 2010, 11:1272-1279.
    • (2010) Traffic , vol.11 , pp. 1272-1279
    • Harris, K.P.1    Tepass, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.