{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T21:51:05Z","timestamp":1790632265878,"version":"4.1.0"},"reference-count":40,"publisher":"Portland Press Ltd.","issue":"6","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2005,10,26]]},"abstract":"<jats:p>Actin reorganization is a tightly regulated process that co-ordinates complex cellular events, such as cell migration, chemotaxis, phagocytosis and adhesion, but the molecular mechanisms that underlie these processes are not well understood. SCAR (suppressor of cAMP receptor)\/WAVE [WASP (Wiskott\u2013Aldrich syndrome protein)-family verprolin homology protein] proteins are members of the conserved WASP family of cytoskeletal regulators, which play a critical role in actin dynamics by triggering Arp2\/3 (actin-related protein 2\/3)-dependent actin nucleation. SCAR\/WAVEs are thought to be regulated by a pentameric complex which also contains Abi (Abl-interactor), Nap (Nck-associated protein), PIR121 (p53-inducible mRNA 121) and HSPC300 (haematopoietic stem progenitor cell 300), but the structural organization of the complex and the contribution of its individual components to the regulation of SCAR\/WAVE function remain unclear. Additional features of SCAR\/WAVE regulation are highlighted by the discovery of other interactors and distinct complexes. It is likely that the combinatorial assembly of different components of SCAR\/WAVE complexes will prove to be vital for their roles at the centre of dynamic actin reorganization.<\/jats:p>","DOI":"10.1042\/bst0331243","type":"journal-article","created":{"date-parts":[[2015,8,11]],"date-time":"2015-08-11T16:17:23Z","timestamp":1439309843000},"page":"1243-1246","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":71,"title":["Regulation of actin assembly by SCAR\/WAVE proteins"],"prefix":"10.1042","volume":"33","author":[{"given":"N.","family":"Ibarra","sequence":"first","affiliation":[{"name":"School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Pollitt","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R.H.","family":"Insall","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2005,10,26]]},"reference":[{"key":"2021111719542596600_B1","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1083\/jcb.142.5.1325","volume":"142","author":"Bear","year":"1998","journal-title":"J. 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