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Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP.

Cory, GO; Cramer, R; Blanchoin, L; Ridley, AJ; (2003) Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol Cell , 11 (5) pp. 1229-1239.

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Abstract

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.

Type: Article
Title: Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP.
Location: United States
Keywords: 3T3 Cells, Actin-Related Protein 2, Actin-Related Protein 3, Actins, Amino Acid Sequence, Animals, Antibody Specificity, Binding Sites, COS Cells, Cytoskeletal Proteins, Eukaryotic Cells, Mice, Nerve Tissue Proteins, Phosphorylation, Polymers, Protein Structure, Tertiary, Proteins, Serine, Up-Regulation, Wiskott-Aldrich Syndrome Protein, Wiskott-Aldrich Syndrome Protein, Neuronal
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)
URI: http://discovery.ucl.ac.uk/id/eprint/185580
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