PubMed Journals: Mol Cell
Source: PMID: 12769847
⇦ ⇨ Mol Cell. 2003 May;11(5):1229-39.
Phosphorylation of the WASP-VCA domain increases
its affinity for the Arp2/3 complex and
enhances actin polymerization by WASP.
Cory GO(1), Cramer R, Blanchoin L, Ridley
(1) Ludwig Institute for Cancer Research,
Royal Free and University College Medical School
Branch, Courtauld Building, 91 Riding House
Street, London W1W 7BS, United Kingdom.
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
PMID: 12769847 [Indexed for MEDLINE]