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Structure and control of the actin regulatory WAVE complex
Journal article   Open access   Peer reviewed

Structure and control of the actin regulatory WAVE complex

Zhucheng Chen, Dominika Borek, Shae B Padrick, Timothy S Gomez, Zoltan Metlagel, Ayman M Ismail, Junko Umetani, Daniel D Billadeau, Zbyszek Otwinowski and Michael K Rosen
Nature (London), v 468(7323), pp 533-538
25 Nov 2010
PMID: 21107423
url
https://europepmc.org/articles/pmc3085272View
Accepted (AM) Open

Abstract

Actins - metabolism Animals HeLa Cells Humans Insecta - cytology Models, Molecular Phosphorylation Protein Structure, Quaternary rac1 GTP-Binding Protein - metabolism Wiskott-Aldrich Syndrome Protein Family - chemistry
Members of the Wiskott-Aldrich syndrome protein (WASP) family control cytoskeletal dynamics by promoting actin filament nucleation with the Arp2/3 complex. The WASP relative WAVE regulates lamellipodia formation within a 400-kilodalton, hetero-pentameric WAVE regulatory complex (WRC). The WRC is inactive towards the Arp2/3 complex, but can be stimulated by the Rac GTPase, kinases and phosphatidylinositols. Here we report the 2.3-ångstrom crystal structure of the WRC and complementary mechanistic analyses. The structure shows that the activity-bearing VCA motif of WAVE is sequestered by a combination of intramolecular and intermolecular contacts within the WRC. Rac and kinases appear to destabilize a WRC element that is necessary for VCA sequestration, suggesting the way in which these signals stimulate WRC activity towards the Arp2/3 complex. The spatial proximity of the Rac binding site and the large basic surface of the WRC suggests how the GTPase and phospholipids could cooperatively recruit the complex to membranes.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
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