{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T13:03:06Z","timestamp":1792501386342,"version":"4.5.0"},"reference-count":56,"publisher":"Rockefeller University Press","issue":"6","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1999,9,20]]},"abstract":"<jats:p>To propel itself in infected cells, the pathogen Shigella flexneri subverts the Cdc42-controlled machinery responsible for actin assembly during filopodia formation. Using a combination of bacterial motility assays in platelet extracts with Escherichia coli expressing the Shigella IcsA protein and in vitro analysis of reconstituted systems from purified proteins, we show here that the bacterial protein IcsA binds N-WASP and activates it in a Cdc42-like fashion. Dramatic stimulation of actin assembly is linked to the formation of a ternary IcsA\u2013N-WASP\u2013Arp2\/3 complex, which nucleates actin polymerization. The Arp2\/3 complex is essential in initiation of actin assembly and Shigella movement, as previously observed for Listeria monocytogenes. Activation of N-WASP by IcsA unmasks two domains acting together in insertional actin polymerization. The isolated COOH-terminal domain of N-WASP containing a verprolin-homology region, a cofilin-homology sequence, and an acidic terminal segment (VCA) interacts with G-actin in a unique profilin-like functional fashion. Hence, when N-WASP is activated, its COOH-terminal domain feeds barbed end growth of filaments and lowers the critical concentration at the bacterial surface. On the other hand, the NH2-terminal domain of N-WASP interacts with F-actin, mediating the attachment of the actin tail to the bacterium surface. VASP is not involved in Shigella movement, and the function of profilin does not require its binding to proline-rich regions.<\/jats:p>","DOI":"10.1083\/jcb.146.6.1319","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T12:45:41Z","timestamp":1027687541000},"page":"1319-1332","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":495,"title":["Activation of the Cdc42 Effector N-Wasp by the\n                    <i>Shigella flexneri<\/i>\n                    Icsa Protein Promotes Actin Nucleation by Arp2\/3 Complex and Bacterial Actin-Based Motility"],"prefix":"10.1083","volume":"146","author":[{"given":"Coumaran","family":"Egile","sequence":"first","affiliation":[{"name":"bUnit\u00e9 de Pathog\u00e9nie Microbienne Mol\u00e9culaire, INSERM U 389, Institut Pasteur, 75724 Paris Cedex 15"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas P.","family":"Loisel","sequence":"additional","affiliation":[{"name":"cDynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique, Gif-sur-Yvette, 91198 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Val\u00e9rie","family":"Laurent","sequence":"additional","affiliation":[{"name":"cDynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique, Gif-sur-Yvette, 91198 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rong","family":"Li","sequence":"additional","affiliation":[{"name":"aDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Pantaloni","sequence":"additional","affiliation":[{"name":"cDynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique, Gif-sur-Yvette, 91198 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe J.","family":"Sansonetti","sequence":"additional","affiliation":[{"name":"bUnit\u00e9 de Pathog\u00e9nie Microbienne Mol\u00e9culaire, INSERM U 389, Institut Pasteur, 75724 Paris Cedex 15"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-France","family":"Carlier","sequence":"additional","affiliation":[{"name":"cDynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique, Gif-sur-Yvette, 91198 France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1999,9,20]]},"reference":[{"key":"2023072901253875600_Abdul-Mananetal1999","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/20726","article-title":"Structure of Cdc42 in complex with the GTPase-binding domain of the Wiskott-Aldrich syndrome protein","volume":"399","author":"Abdul-Manan","year":"1999","journal-title":"Nature."},{"key":"2023072901253875600_Baillyetal1999","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1083\/jcb.145.2.331","article-title":"Relationship between Arp2\/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after EGF stimulation","volume":"145","author":"Bailly","year":"1999","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Bearetal1998","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1083\/jcb.142.5.1325","article-title":"SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development","volume":"142","author":"Bear","year":"1998","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Beckerle1998","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/S0092-8674(00)81697-9","article-title":"Spatial control of actin filament assemblylessons from Listeria","volume":"95","author":"Beckerle","year":"1998","journal-title":"Cell."},{"key":"2023072901253875600_Bernardinietal1989","doi-asserted-by":"crossref","first-page":"3867","DOI":"10.1073\/pnas.86.10.3867","article-title":"Identification of IcsA, a plasmid locus of Shigella flexneri that governs bacterial intra and intercellular spread through interaction with F-actin","volume":"86","author":"Bernardini","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2023072901253875600_BiandZigmond1999","doi-asserted-by":"crossref","first-page":"R160","DOI":"10.1016\/S0960-9822(99)80102-X","article-title":"Actin polymerizationwhere the WASP stings","volume":"9","author":"Bi","year":"1999","journal-title":"Curr. Biol."},{"key":"2023072901253875600_Bjorkegren-Sjogrenetal1997","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/S0014-5793(97)01376-8","article-title":"Isolation and characterization of two mutants of human profilin I that do not bind poly(l-proline)","volume":"418","author":"Bjorkegren-Sjogren","year":"1997","journal-title":"FEBS Lett."},{"key":"2023072901253875600_Carlier1998","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0955-0674(98)80085-9","article-title":"Control of actin dynamics","volume":"10","author":"Carlier","year":"1998","journal-title":"Curr. Opin. Cell Biol."},{"key":"2023072901253875600_Carlieretal1997","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1083\/jcb.136.6.1307","article-title":"ADF\/cofilin enhances the turnover of actin filaments. Implication in actin-based motility","volume":"136","author":"Carlier","year":"1997","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Casellaetal1986","doi-asserted-by":"crossref","first-page":"10915","DOI":"10.1016\/S0021-9258(18)67474-5","article-title":"Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments","volume":"261","author":"Casella","year":"1986","journal-title":"J. Biol. Chem."},{"key":"2023072901253875600_Derryetal1994","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/0092-8674(94)90528-2","article-title":"Isolation of a novel gene mutated in Wiskott-Aldrich syndrome","volume":"78","author":"Derry","year":"1994","journal-title":"Cell."},{"key":"2023072901253875600_Domannetal1992","doi-asserted-by":"crossref","first-page":"1981","DOI":"10.1002\/j.1460-2075.1992.tb05252.x","article-title":"A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin","volume":"11","author":"Domann","year":"1992","journal-title":"EMBO (Eur. Mol. Biol. Organ.) J."},{"key":"2023072901253875600_Goldberg1997","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1002\/(SICI)1097-0169(1997)37:1<44::AID-CM5>3.0.CO;2-H","article-title":"Shigella actin-based motility in the absence of vinculin","volume":"37","author":"Goldberg","year":"1997","journal-title":"Cell Motil. Cytoskeleton."},{"key":"2023072901253875600_GoldbergandTheriot1995","doi-asserted-by":"crossref","first-page":"6572","DOI":"10.1073\/pnas.92.14.6572","article-title":"Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility","volume":"92","author":"Goldberg","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2023072901253875600_Goldbergetal1993","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.1128\/jb.175.8.2189-2196.1993","article-title":"Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement","volume":"175","author":"Goldberg","year":"1993","journal-title":"J. Bacteriol."},{"key":"2023072901253875600_Gutsche-Perelroizenetal1999","doi-asserted-by":"crossref","first-page":"6234","DOI":"10.1074\/jbc.274.10.6234","article-title":"Filament assembly from profilin-actin","volume":"274","author":"Gutsche-Perelroizen","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2023072901253875600_HigleyandWay1997","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/S0955-0674(97)80153-6","article-title":"Actin and cell pathogenesis","volume":"9","author":"Higley","year":"1997","journal-title":"Curr. Opin. Cell Biol."},{"key":"2023072901253875600_Kocksetal1992","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/0092-8674(92)90188-I","article-title":"L. monocytogenes-induced assembly requires actA gene product, a surface protein","volume":"68","author":"Kocks","year":"1992","journal-title":"Cell."},{"key":"2023072901253875600_Kocksetal1995","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1111\/j.1365-2958.1995.mmi_18030413.x","article-title":"The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocua and E. coli respectively","volume":"18","author":"Kocks","year":"1995","journal-title":"Mol. Microbiol."},{"key":"2023072901253875600_Kozmaetal1995","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1128\/MCB.15.4.1942","article-title":"The ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts","volume":"15","author":"Kozma","year":"1995","journal-title":"Mol. Cell. Biol."},{"key":"2023072901253875600_Laineetal1997","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1083\/jcb.138.6.1255","article-title":"Vinculin proteolysis unmasks an ActA homolog for actin-based Shigella motility","volume":"138","author":"Laine","year":"1997","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_LaurentandCarlier1997","first-page":"359","article-title":"Use of platelet extracts for actin-based motility of Listeria monocytogenes","volume-title":"Cell Biology Laboratory Handbook","author":"Laurent","year":"1997"},{"key":"2023072901253875600_Laurentetal1999","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1083\/jcb.144.6.1245","article-title":"Role of the proteins of the Ena\/VASP family in actin-based motility of Listeria monocytogenes","volume":"144","author":"Laurent","year":"1999","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_LechlerandLi1997","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1083\/jcb.138.1.95","article-title":"In vitro reconstitution of cortical actin assembly sites in budding yeast","volume":"138","author":"Lechler","year":"1997","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Lettetal1989","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1128\/jb.171.1.353-359.1989","article-title":"VirG, a plasmid-coded virulence gene of Shigella flexneriidentification of the virG protein and determination of the complete coding sequence","volume":"171","author":"Lett","year":"1989","journal-title":"J. Bacteriol."},{"key":"2023072901253875600_Li1997","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1083\/jcb.136.3.649","article-title":"Bee1, a yeast protein with homology to Wiskott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton","volume":"136","author":"Li","year":"1997","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Loiseletal1999","article-title":"Reconstitution of actin-based motility of Listeria and Shigella from pure proteins","volume":"In press","author":"Loisel","year":"1999","journal-title":"Nature"},{"key":"2023072901253875600_Maetal1998a","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1083\/jcb.140.5.1125","article-title":"Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts","volume":"140","author":"Ma","year":"1998","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Maetal1998b","doi-asserted-by":"crossref","first-page":"15362","DOI":"10.1073\/pnas.95.26.15362","article-title":"The Arp2\/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42","volume":"95","author":"Ma","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2023072901253875600_MacheskyandInsall1998","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1016\/S0960-9822(98)00015-3","article-title":"Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2\/3 complex","volume":"8","author":"Machesky","year":"1998","journal-title":"Curr. Biol."},{"key":"2023072901253875600_Macheskyetal1999","doi-asserted-by":"crossref","first-page":"3739","DOI":"10.1073\/pnas.96.7.3739","article-title":"Scar, a WASp-related protein, activates dendritic nucleation of actin filaments by the Arp2\/3 complex","volume":"96","author":"Machesky","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2023072901253875600_Marchandetal1995","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1083\/jcb.130.2.331","article-title":"Actin-based movement of Listeria monocytogenes in Xenopus egg extracts is due to the maintenance of uncapped barbed ends at the bacterium surface","volume":"130","author":"Marchand","year":"1995","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_MikiandTakenawa1998","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1006\/bbrc.1997.8064","article-title":"Direct binding of the verprolin-hology domain in N-WASP to actin is essential for cytoskeletal reorganization","volume":"243","author":"Miki","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2023072901253875600_Mikietal1996","doi-asserted-by":"crossref","first-page":"5326","DOI":"10.1002\/j.1460-2075.1996.tb00917.x","article-title":"N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases","volume":"15","author":"Miki","year":"1996","journal-title":"EMBO (Eur. Mol. Biol. Organ.) J."},{"key":"2023072901253875600_Mikietal1998a","doi-asserted-by":"crossref","first-page":"6932","DOI":"10.1093\/emboj\/17.23.6932","article-title":"WAVE, a novel WASP-family protein involved in actin reorganization induced by rac","volume":"17","author":"Miki","year":"1998","journal-title":"EMBO (Eur. Mol. Biol. Organ.) J."},{"key":"2023072901253875600_Mikietal1998b","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1038\/34208","article-title":"Induction of filopodium formation by a N-WASP-related actin-depolymerizing factor","volume":"391","author":"Miki","year":"1998","journal-title":"Nature."},{"key":"2023072901253875600_Mounieretal1999","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1242\/jcs.112.13.2069","article-title":"Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility","volume":"112","author":"Mounier","year":"1999","journal-title":"J. Cell Sci."},{"key":"2023072901253875600_Mullinsetal1998","doi-asserted-by":"crossref","first-page":"6181","DOI":"10.1073\/pnas.95.11.6181","article-title":"The interaction of Arp2\/3 complex with actinnucleation, high affinity pointed end capping and formation of branching networks of actin filaments","volume":"95","author":"Mullins","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2023072901253875600_NhieuandSansonetti1999","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S1369-5274(99)80009-5","article-title":"Mechanism of Shigella entry into epithelial cells","volume":"2","author":"Nhieu","year":"1999","journal-title":"Curr. Opin. Microbiol."},{"key":"2023072901253875600_Niebuhretal1997","doi-asserted-by":"crossref","first-page":"5433","DOI":"10.1093\/emboj\/16.17.5433","article-title":"A novel proline-rich motif present in ActA and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena\/VASP family","volume":"16","author":"Niebuhr","year":"1997","journal-title":"EMBO (Eur. Mol. Biol. Organ.) J."},{"key":"2023072901253875600_NobesandHall1995","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0092-8674(95)90370-4","article-title":"Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia","volume":"81","author":"Nobes","year":"1995","journal-title":"Cell."},{"key":"2023072901253875600_PantaloniandCarlier1993","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/0092-8674(93)90544-Z","article-title":"How profilin promotes actin filament assembly in the presence of thymosin \u03b24","volume":"75","author":"Pantaloni","year":"1993","journal-title":"Cell."},{"key":"2023072901253875600_Prevostetal1992","doi-asserted-by":"crossref","first-page":"4088","DOI":"10.1128\/iai.60.10.4088-4099.1992","article-title":"Unipolar reorganization of F-actin layer at bacterial division and bundling of actin filaments by plastin correlate with movement of Shigella flexneri within HeLa cells","volume":"60","author":"Prevost","year":"1992","journal-title":"Infect. Immun."},{"key":"2023072901253875600_Rameshetal1999","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0962-8924(98)01411-1","article-title":"Waltzing with WASP","volume":"9","author":"Ramesh","year":"1999","journal-title":"Trends Cell Biol."},{"key":"2023072901253875600_Ressadetal1999","doi-asserted-by":"crossref","first-page":"20970","DOI":"10.1074\/jbc.274.30.20970","article-title":"Control of the turnover and length distribution of actin filaments by ADF\/cofilin in the presence of capping proteins and Arp2\/3 complex","volume":"274","author":"Ressad","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2023072901253875600_Rohatgietal1999","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0092-8674(00)80732-1","article-title":"The interaction between N-WASP and the Arp2\/3 complex links Cdc42-dependent signals to actin assembly","volume":"97","author":"Rohatgi","year":"1999","journal-title":"Cell."},{"key":"2023072901253875600_Smithetal1996","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1083\/jcb.135.3.647","article-title":"The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of VASP and profilin","volume":"135","author":"Smith","year":"1996","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Suetsuguetal1998","doi-asserted-by":"crossref","first-page":"6516","DOI":"10.1093\/emboj\/17.22.6516","article-title":"The essential role of profilin in the assembly of actin for microspike formation","volume":"17","author":"Suetsugu","year":"1998","journal-title":"EMBO (Eur. Mol. Biol. Organ.) J."},{"key":"2023072901253875600_Suzukietal1996","doi-asserted-by":"crossref","first-page":"21878","DOI":"10.1074\/jbc.271.36.21878","article-title":"Functional analysis of Shigella VirG domains essential for interaction with vinculin and actin-based motility","volume":"271","author":"Suzuki","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2023072901253875600_Suzukietal1998","doi-asserted-by":"crossref","first-page":"2767","DOI":"10.1093\/emboj\/17.10.2767","article-title":"Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri","volume":"17","author":"Suzuki","year":"1998","journal-title":"EMBO (Eur. Mol. Biol. Organ.) J."},{"key":"2023072901253875600_SvitkinaandBorisy1999","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1083\/jcb.145.5.1009","article-title":"Arp2\/3 complex and actin depolymerizing factor\/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia","volume":"145","author":"Svitkina","year":"1999","journal-title":"J. Cell Biol."},{"key":"2023072901253875600_Welchetal1997","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/385265a0","article-title":"Actin polymerization is induced by the Arp2\/3 complex at the surface of Listeria monocytogenes","volume":"385","author":"Welch","year":"1997","journal-title":"Nature."},{"key":"2023072901253875600_Welchetal1998","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1126\/science.281.5373.105","article-title":"Interaction of human Arp2\/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation","volume":"281","author":"Welch","year":"1998","journal-title":"Science."},{"key":"2023072901253875600_Winteretal1999","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/S0960-9822(99)80218-8","article-title":"Activation of the Arp2\/3 complex by Bee1p, a WASP-family protein","volume":"9","author":"Winter","year":"1999","journal-title":"Curr. Biol."},{"key":"2023072901253875600_Zeileetal1998","doi-asserted-by":"crossref","first-page":"13917","DOI":"10.1073\/pnas.95.23.13917","article-title":"Vaccinia locomotion in host cellsevidence for the universal involvement of actin-based motility sequences ABM-1 and ABM-2","volume":"95","author":"Zeile","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2023072901253875600_Zigmondetal1998","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1083\/jcb.142.4.1001","article-title":"Mechanism of Cdc42-induced actin polymerization in neutrophil extracts","volume":"142","author":"Zigmond","year":"1998","journal-title":"J. Cell Biol."}],"container-title":["The Journal of Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/146\/6\/1319\/1854079\/9905089.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/146\/6\/1319\/1854079\/9905089.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,28]],"date-time":"2023-07-28T21:26:19Z","timestamp":1690579579000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/146\/6\/1319\/31991\/Activation-of-the-Cdc42-Effector-N-Wasp-by-the"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,9,20]]},"references-count":56,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1999,9,20]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.146.6.1319","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1999,9,20]]}}}