[HTML][HTML] Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation
GOC Cory, R Garg, R Cramer, AJ Ridley - Journal of Biological Chemistry, 2002 - ASBMB
Wiskott-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 …
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 …