Linked Life Data

12235133

Source:http://linkedlifedata.com/resource/pubmed/id/12235133

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pubmed-article:12235133pubmed:abstractTextWiskott-Aldrich Syndrome protein (WASp) is a key regulator of the Arp2/3 complex and the actin cytoskeleton in hematopoietic cells. WASp is capable of forming an auto-inhibited conformation, which can be disrupted by binding of Cdc42 and phosphatidylinositol 4,5-bisphosphate, leading to its activation. Stimulation of the collagen receptor on platelets and crosslinking the B-cell receptor induce tyrosine phosphorylation of WASp. Here we show that the Src family kinase Hck induces phosphorylation of WASp-Tyr(291) independently of Cdc42 and that this causes a shift in the mobility of WASp upon SDS-PAGE. A phospho-mimicking mutant, WASp-Y291E, exhibited an enhanced ability to stimulate actin polymerization in a cell-free system and when microinjected into primary macrophages induced extensive filopodium formation with greater efficiency than wild-type WASp or a Y291F mutant. We propose that phosphorylation of Tyr(291) directly regulates WASp function.lld:pubmed
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pubmed-article:12235133pubmed:pagination45115-21lld:pubmed
pubmed-article:12235133pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:12235133pubmed:articleTitlePhosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.lld:pubmed
pubmed-article:12235133pubmed:affiliationLudwig Institute for Cancer Research, Royal Free and University College Medical School Branch, Courtauld Building, 91 Riding House Street, London W1W 7BS, United Kingdom.lld:pubmed
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