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			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
			AJ.

			Author Information
			(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
			by WASP.

			PMID: 12769847 [Indexed for MEDLINE]

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