Phosphorylation of the WASP-VCA Domain Increases Its Affinity for the Arp2/3 Complex and Enhances Actin Polymerization by WASP

Wiskott-Aldrich syndrome protein (WASP) and neural (N)-WASP regulate dynamic actin structures through the ability of their VCA domains to bind to and stimulate the actin nucleating activity of the Arp2/3 complex. Here we identify two phosphorylation sites in the VCA domain of WASP at serines 483 and...

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Bibliographic Details
Published in:Molecular cell 2003-05, Vol.11 (5), p.1229-1239
Main Authors: Cory, Giles O.C., Cramer, Rainer, Blanchoin, Laurent, Ridley, Anne J.
Format: Article
Language:English
Subjects:
3T3 Cells
Actin-Related Protein 2
Actin-Related Protein 3
Actins - biosynthesis
Amino Acid Sequence - genetics
Animals
Antibody Specificity - immunology
Binding Sites - genetics
COS Cells
Cytoskeletal Proteins - genetics
Cytoskeletal Proteins - metabolism
Eukaryotic Cells - metabolism
Life Sciences
Mice
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Phosphorylation
Polymers - metabolism
Protein Structure, Tertiary - genetics
Proteins - genetics
Proteins - metabolism
Serine - metabolism
Up-Regulation - genetics
Wiskott-Aldrich Syndrome Protein
Wiskott-Aldrich Syndrome Protein, Neuronal
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Summary:Wiskott-Aldrich syndrome protein (WASP) and neural (N)-WASP regulate dynamic actin structures through the ability of their VCA domains to bind to and stimulate the actin nucleating activity of the Arp2/3 complex. Here we identify two phosphorylation sites in the VCA domain of WASP at serines 483 and 484. S483 and S484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the VCA domain for the Arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length WASP molecule. We propose that constitutive VCA domain phosphorylation is required for optimal stimulation of the Arp2/3 complex by WASP.
ISSN:1097-2765
1097-4164
DOI:10.1016/S1097-2765(03)00172-2