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Article

Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.

The Journal of biological chemistry - 22 Nov 2002

Cory Giles O C, Garg Ritu, Cramer Rainer, Ridley Anne J

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 12235133
DOI: 10.1074/jbc.M203346200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.PMID 12235133Read ↗

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Understanding immunoactinopathies: A decade of research on WAS gene defects.Semantic proximity Read ↗

New Structural Insights into Formation of the Key Actin Regulating WIP-WASp Complex Determined by NMR and Molecular Imaging.Semantic proximity Read ↗

Wiskott-Aldrich Syndrome: a model for defective actin reorganization, cell trafficking and synapse formation.Semantic proximity Read ↗

N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases.Semantic proximity Read ↗

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