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dc.contributor.authorPocha, SM
dc.contributor.authorCory, GO
dc.date.accessioned2013-11-14T14:12:22Z
dc.date.issued2009-01
dc.description.abstractThe (Wiskott-Aldrich Syndrome Protein)-family verprolin homologous protein (WAVE) family of proteins occupies a pivotal position in the cell, converting extracellular signals into the formation of branched filamentous (F) actin structures. WAVE proteins contain a verprolin central acidic (VCA) domain at their C-terminus, responsible for binding to and activating the Arp2/3 complex, which in-turn nucleates the formation of new actin filaments. Here we identify five Casein Kinase 2 (CK2) phosphorylation sites within the VCA domain of WAVE2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the Arp2/3 complex. Phosphorylation of ser 482 and 484 specifically inhibits the activation of the Arp2/3 complex by the WAVE2 VCA domain, but has no effect on the affinity for the Arp2/3 complex when the other phosphorylation sites are occupied. We demonstrate phosphorylation of all five sites on endogenous WAVE2 and show that their mutation to non-phosphorylatable alanine residues inhibits WAVE2 function in vivo, inhibiting cell ruffling and disrupting the integrity of the leading edge of migrating cells.en_GB
dc.identifier.citationCell Motility and the Cytoskeleton, 2009, Vol. 66, Issue 1, pp. 36 - 47en_GB
dc.identifier.doi10.1002/cm.20323
dc.identifier.urihttp://hdl.handle.net/10871/13949
dc.language.isoenen_GB
dc.publisherWiley-Blackwellen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/19012317en_GB
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1002/cm.20323/abstracten_GB
dc.subjectActin-Related Protein 2-3 Complexen_GB
dc.subjectAmino Acid Sequenceen_GB
dc.subjectAnimalsen_GB
dc.subjectCOS Cellsen_GB
dc.subjectCasein Kinase IIen_GB
dc.subjectCell Movementen_GB
dc.subjectCercopithecus aethiopsen_GB
dc.subjectHumansen_GB
dc.subjectMiceen_GB
dc.subjectMitogen-Activated Protein Kinasesen_GB
dc.subjectMolecular Sequence Dataen_GB
dc.subjectNIH 3T3 Cellsen_GB
dc.subjectPhosphorylationen_GB
dc.subjectProtein Kinase Inhibitorsen_GB
dc.subjectProtein Structure, Tertiaryen_GB
dc.subjectPseudopodiaen_GB
dc.subjectRatsen_GB
dc.subjectWiskott-Aldrich Syndrome Protein Familyen_GB
dc.titleWAVE2 is regulated by multiple phosphorylation events within its VCA domain.en_GB
dc.typeArticleen_GB
dc.date.available2013-11-14T14:12:22Z
dc.identifier.issn0886-1544
exeter.place-of-publicationUnited States
dc.descriptionaddresses: Department of Biochemistry, Faculty of Medical and Veterinary Sciences, University of Bristol, Bristol, United Kingdom.en_GB
dc.descriptionnotes: PMCID: PMC2798068en_GB
dc.descriptionOnlineOpen Article. This is a copy of an article published in Cell Motility and the Cytoskeleton. This journal is available online at: http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1949-3592en_GB
dc.descriptionThe definitive version is available at www3.interscience.wiley.comen_GB
dc.identifier.journalCell Motility and the Cytoskeletonen_GB


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