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Beads coated with the VCA domain of the Wiskott\/Aldrich-syndrome protein (WASP) recruit the actin-nucleating Arp2\/3 complex, polymerize actin at their surface and undergo movement when placed in cell-free extracts. T-Plastin increased the velocity of VCA beads 1.5 times, stabilized actin comets and concomitantly displaced cofilin, an actin-depolymerizing protein. T-Plastin also decreased the F-actin disassembly rate and inhibited cofilin-mediated depolymerization of actin filaments in vitro. Importantly, a bundling-incompetent variant comprising the first actin-binding domain (ABD1) had similar effects. In cells, this domain induced the formation of long actin cables to which other actin-regulating proteins were recruited. Altogether, these results favor a mechanism in which binding of ABD1 controls actin turnover independently of cross-link formation. In vivo, this activity might contribute to the assembly and maintenance of the actin cytoskeleton of plasma-membrane protrusions.<\/jats:p>","DOI":"10.1242\/jcs.01698","type":"journal-article","created":{"date-parts":[[2005,3,1]],"date-time":"2005-03-01T22:38:18Z","timestamp":1109716698000},"page":"1255-1265","source":"Crossref","is-referenced-by-count":74,"title":["Actin-filament cross-linking protein T-plastin increases Arp2\/3-mediated actin-based movement"],"prefix":"10.1242","volume":"118","author":[{"given":"Adeline","family":"Giganti","sequence":"first","affiliation":[{"name":"Laboratoire de Biologie Mole\u0301culaire, d'Analyse Ge\u0301nique et de Mode\u0301lisation, Centre de Recherche Public-Sante\u0301, 42, rue du Laboratoire, L-1911, Luxembourg"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie","family":"Plastino","sequence":"additional","affiliation":[{"name":"Laboratoire Physicochimie `Curie', UMR168 CNRS\/Institut Curie, 11, rue Pierre et Marie Curie, 75231 Paris Cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bassam","family":"Janji","sequence":"additional","affiliation":[{"name":"Laboratoire de Biologie Mole\u0301culaire, d'Analyse Ge\u0301nique et de Mode\u0301lisation, Centre de Recherche Public-Sante\u0301, 42, rue du Laboratoire, L-1911, Luxembourg"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marleen","family":"Van Troys","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, and Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB09), Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Delphine","family":"Lentz","sequence":"additional","affiliation":[{"name":"Laboratoire de Biologie Mole\u0301culaire, d'Analyse Ge\u0301nique et de Mode\u0301lisation, Centre de Recherche Public-Sante\u0301, 42, rue du Laboratoire, L-1911, Luxembourg"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Ampe","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, and Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB09), Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ce\u0301cile","family":"Sykes","sequence":"additional","affiliation":[{"name":"Laboratoire Physicochimie `Curie', UMR168 CNRS\/Institut Curie, 11, rue Pierre et Marie Curie, 75231 Paris Cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evelyne","family":"Friederich","sequence":"additional","affiliation":[{"name":"Laboratoire de Biologie Mole\u0301culaire, d'Analyse Ge\u0301nique et de Mode\u0301lisation, Centre de Recherche Public-Sante\u0301, 42, rue du Laboratoire, L-1911, Luxembourg"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042519210067700_REF1","doi-asserted-by":"crossref","unstructured":"Adam, T., Arpin, M., Prevost, M. 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