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Arp2/3 complex is bound and activated by two WASP proteins
Journal article   Open access   Peer reviewed

Arp2/3 complex is bound and activated by two WASP proteins

Shae B. Padrick, Lynda K. Doolittle, Chad A. Brautigam, David S. King and Michael K. Rosen
Proceedings of the National Academy of Sciences - PNAS, v 108(33), pp E472-E479
16 Aug 2011
PMID: 21676863
url
https://doi.org/10.1073/pnas.1100236108View
Published, Version of Record (VoR) Open

Abstract

actin dynamics Biological Sciences molecular mechanism PNAS Plus
Actin related protein 2/actin related protein 3 (Arp2/3) complex nucleates new actin filaments in eukaryotic cells in response to signals from proteins in the Wiskott–Aldrich syndrome protein (WASP) family. The conserved VCA domain of WASP proteins activates Arp2/3 complex by inducing conformational changes and delivering the first actin monomer of the daughter filament. Previous models of activation have invoked a single VCA acting at a single site on Arp2/3 complex. Here we show that activation most likely involves engagement of two distinct sites on Arp2/3 complex by two VCA molecules, each delivering an actin monomer. One site is on Arp3 and the second is on ARPC1 and Arp2. The VCAs at these sites have distinct roles in activation. Our findings reconcile apparently conflicting literature on VCA activation of Arp2/3 complex and lead to a new model for this process.

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