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Pollard T.D., Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:2003;453-465 This excellent review provides a comprehensive view of the current knowledge of how actin dynamics drive cell motility.
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Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
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This article is the first to identify the protein complex that inhibits the activity of Scar/WAVE1 in cells. It also provides the basic mechanism of Scar/WAVE activation through signal-dependent dissociation of this complex.
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Eden S., Rohatgi R., Podtelejnikov A.V., Mann M., Kirschner M.W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature. 418:2002;790-793 This article is the first to identify the protein complex that inhibits the activity of Scar/WAVE1 in cells. It also provides the basic mechanism of Scar/WAVE activation through signal-dependent dissociation of this complex.
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Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
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Winter D.C., Choe E.Y., Li R. Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc Natl Acad Sci U S A. 96:1999;7288-7293
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Essential role of the C. elegans Arp2/3 complex in cell migration during ventral enclosure
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This article provides in vivo evidence for the requirement for Arp2/3-complex-mediated actin polymerization during cell motility. By using RNAi-mediated depletion of Arp2/3 complex subunits and WASP the authors show that these proteins play a key role in ventral enclosure in C. elegans.
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Sawa M., Suetsugu S., Sugimoto A., Miki H., Yamamoto M., Takenawa T. Essential role of the C. elegans Arp2/3 complex in cell migration during ventral enclosure. J Cell Sci. 116:2003;1505-1518 This article provides in vivo evidence for the requirement for Arp2/3-complex-mediated actin polymerization during cell motility. By using RNAi-mediated depletion of Arp2/3 complex subunits and WASP the authors show that these proteins play a key role in ventral enclosure in C. elegans.
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A Formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans
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Severson A.F., Baillie D.L., Bowerman B. A Formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans. Curr Biol. 12:2002;2066-2075
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SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila
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Using a genetic approach, SCAR is shown to be a more important regulator of the Arp2/3 complex during morphological processes in Drosophila than WASP. This article highlights the distinct roles of WASP and Scar/WAVE proteins in different cellular processes.
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Zallen J.A., Cohen Y., Hudson A.M., Cooley L., Wieschaus E., Schejter E.D. SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila. J Cell Biol. 156:2002;689-701 Using a genetic approach, SCAR is shown to be a more important regulator of the Arp2/3 complex during morphological processes in Drosophila than WASP. This article highlights the distinct roles of WASP and Scar/WAVE proteins in different cellular processes.
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A subset of dynamic actin rearrangements in Drosophila requires the Arp2/3 complex
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Hudson A.M., Cooley L. A subset of dynamic actin rearrangements in Drosophila requires the Arp2/3 complex. J Cell Biol. 156:2002;677-687
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Harborth J., Elbashir S.M., Bechert K., Tuschl T., Weber K. Identification of essential genes in cultured mammalian cells using small interfering RNAs. J Cell Sci. 114:2001;4557-4565
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0037704913
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Mutations in actin-related proteins 2 and 3 affect cell shape development in Arabidopsis
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Mathur J., Mathur N., Kernebeck B., Hulskamp M. Mutations in actin-related proteins 2 and 3 affect cell shape development in Arabidopsis. Plant Cell. 15:2003;1632-1645
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Mathur, J.1
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Analysis of the actin-myosin II system in fish epidermal keratocytes: Mechanism of cell body translocation
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Svitkina T.M., Verkhovsky A.B., Mcquade K.M., Borisy G.G. Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J Cell Biol. 139:1997;397-415
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0141433278
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Molecular requirements for actin-based lamella formation in Drosophila S2 cells
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Using a RNAi-based approach in a new, popular Drosophila cell-culture model, authors study the role of a large number of proteins in lamella formation. This article highlights the role of Scar as a regulator of Arp2/3 activity in the formation of lamellipodia, and shows that the function of the Scar regulatory complex is to inhibit Scar degradation.
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Rogers S.L., Weidemann U., Stuurman N., Vale R.D. Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J Cell Biol. 162:2003;1079-1088 Using a RNAi-based approach in a new, popular Drosophila cell-culture model, authors study the role of a large number of proteins in lamella formation. This article highlights the role of Scar as a regulator of Arp2/3 activity in the formation of lamellipodia, and shows that the function of the Scar regulatory complex is to inhibit Scar degradation.
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Rogers, S.L.1
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0037026486
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Actin dynamics in the contractile ring during cytokinesis in fission yeast
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Using fission yeast as a model system, the authors show that, during cell division, the contractile ring is a dynamic structure in which actin and other ring components assemble and disassemble continuously from the ring. Actin polymerization by both a formin and the Arp2/3 complex appears to play a key role in the cleavage process.
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Pelham R.J., Chang F. Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature. 419:2002;82-86 Using fission yeast as a model system, the authors show that, during cell division, the contractile ring is a dynamic structure in which actin and other ring components assemble and disassemble continuously from the ring. Actin polymerization by both a formin and the Arp2/3 complex appears to play a key role in the cleavage process.
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Pelham, R.J.1
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The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe
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Carnahan R.H., Gould K.L. The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe. J Cell Biol. 162:2003;851-862
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Carnahan, R.H.1
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Stevenson V., Hudson A., Cooley L., Theurkauf W.E. Arp2/3-dependent pseudocleavage furrow assembly in syncytial Drosophila embryos. Curr Biol. 12:2002;705-711
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Conserved interactions with cytoskeletal but not signaling elements are an essential aspect of Drosophila WASP function
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Tal T., Vaizel-Ohayon D., Schejter E.D. Conserved interactions with cytoskeletal but not signaling elements are an essential aspect of Drosophila WASP function. Dev Biol. 243:2002;260-271
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Arabidopsis CROOKED encodes for the smallest subunit of the Arp2/3 complex and controls cell shape by region specific fine F-actin formation
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This is the first article to describe a plant homolog of Arp2/3 complex subunits, and therefore provides evidence for the evolutionarily conserved role of Arp2/3-mediated actin polymerization in very distinct cellular contexts.
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Mathur J., Mathur N., Kirik V., Kernebeck B., Purushottam B., Hulskamp M. Arabidopsis CROOKED encodes for the smallest subunit of the Arp2/3 complex and controls cell shape by region specific fine F-actin formation. Development. 130:2003;3137-3146 This is the first article to describe a plant homolog of Arp2/3 complex subunits, and therefore provides evidence for the evolutionarily conserved role of Arp2/3-mediated actin polymerization in very distinct cellular contexts.
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Requirements for Arabidopsis ATARP2 and ATARP3 during epidermal development
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Le, J.1
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Deeks M.J., Hussey P.J. Arp2/3 and 'The shape of things to come'. Curr Opin Plant Biol. 6:2003;561-567
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A small, novel protein highly conserved in plants and animals promotes the polarized growth and division of maize leaf epidermal cells
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Frank M.J., Smith L.G. A small, novel protein highly conserved in plants and animals promotes the polarized growth and division of maize leaf epidermal cells. Curr Biol. 12:2002;849-853
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Frank M.J., Cartwright H.N., Smith L.G. Three Brick genes have distinct functions in a common pathway promoting polarized cell division and cell morphogenesis in the maize leaf epidermis. Development. 130:2003;753-762
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Rodal A.A., Manning A.L., Goode B.L., Drubin D.G. Negative regulation of yeast WASP by two SH3-domain-containing proteins. Curr Biol. 13:2003;1000-1008
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The GEX-2 and GEX-3 proteins are required for tissue morphogenesis and cell migrations in C. elegans
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WASP, the Drosophila Wiskott-Aldrich syndrome gene homologue, is required for cell fate decisions mediated by Notch signaling
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Ben-Yaacov S., Le Borgne R., Abrahamson I., Scheweisguth F., Schejter E.D. WASP, the Drosophila Wiskott-Aldrich syndrome gene homologue, is required for cell fate decisions mediated by Notch signaling. J Cell Biol. 152:2001;1-13
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Mechanism of filopodia initiation by reorganization of a dendritic network
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Svitkina T.M., Bulanova E.A., Chaga O.Y., Vignjevic D.M., Kojima S., Vasiliev J.M., Borisy G.G. Mechanism of filopodia initiation by reorganization of a dendritic network. J Cell Biol. 160:2003;409-421 How filopodia are initiated has remained a mystery for a long time. By using a combination of microscopical techniques, the authors show that dendritic actin arrays of the lamellipodia can be rearranged to form filopodia.
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Svitkina, T.M.1
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Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
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Lommel S., Benesch S., Rottner K., Franz T., Wehland J., Kuhn R. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2:2001;850-857
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Snapper S.B., Takeshima F., Anton I., Liu C.-H., Thomas S.M., Nguyen D., Dudley D., Fraser H., Purich D., Lopez-Ilasaca M., et al. N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility. Nat Cell Biol. 3:2001;897-904
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WAVE2 deficiency reveals distinct roles in embryogenesis and Rac-mediated actin-based motility
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Yan C., Martinez-Quiles N., Eden S., Shibata T., Takeshima F., Shinkura R., Fujiwara Y., Bronson R., Snapper S.B., Kirschner M.W., et al. WAVE2 deficiency reveals distinct roles in embryogenesis and Rac-mediated actin-based motility. EMBO J. 22:2003;3602-3612
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Differential roles of WAVE1 and WAVE2 in dorsal and peripheral ruffle formation for fibroblast cell migration
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Suetsugu S., Yamazaki D., Kurisu S., Takenawa T. Differential roles of WAVE1 and WAVE2 in dorsal and peripheral ruffle formation for fibroblast cell migration. Dev Cell. 5:2003;595-609
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The WASP homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast
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Naqvi S.N., Zahn R., Mitchell D.A., Stevenson B.J., Munn A.L. The WASP homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Curr Biol. 8:1998;959-962
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Kessels M.M., Qualmann B. Syndapins integrate N-WASP in receptor mediated endocytosis. EMBO J. 21:2002;6083-6094
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Chang F.S., Stefan C.J., Blumer K.J. A WASP homolog powers actin polymerization-dependent motility of endosomes in vivo. Curr Biol. 13:2003;455-463
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Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2
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Benesch S., Lommel S., Steffen A., Stradal T.E.B., Scaplehorn N., Way M., Wehland J., Rottner K. Phosphatidylinositol 4, 5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2. J Biol Chem. 277:2002;37771-37776
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The WASP-like protein Scar regulates macropinocytosis, phagocytosis and endosomal membrane flow in Dictyostelium
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Seastone D.J., Harris E., Temesvari L.A., Bear J.E., Saxe C.L., Cardelli J. The WASP-like protein Scar regulates macropinocytosis, phagocytosis and endosomal membrane flow in Dictyostelium. J Cell Sci. 114:2001;2673-2683
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Notarangelo L.D., Ochs H.D. Wiskott-Aldrich syndrome: a model for defective actin reorganization, cell trafficking and synapse formation. Curr Opin Immunol. 15:2003;585-591
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Badour K., Zhang J., Shi F., McGavin M.K., Ramperstad V., Hardy L.A., Field D., Siminovitch K.A. The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse. Immunity. 18:2003;141-154
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Wiskott-Aldrich syndrome protein is required for NK cell cytotoxicity and colocalizes with actin to NK cell-activating immunological synapses
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Orange J.S., Ramesh N., Remold-O'Donnell E., Sasahara Y., Koopman L., Byrne M., Bonilla F.A., Rosen F.S., Geha R.S., Strominger J.L. Wiskott-Aldrich syndrome protein is required for NK cell cytotoxicity and colocalizes with actin to NK cell-activating immunological synapses. Proc Natl Acad Sci U S A. 99:2002;11351-11356
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