Journal article
Arp2/3 complex is bound and activated by two WASP proteins
Proceedings of the National Academy of Sciences - PNAS, v 108(33), pp E472-E479
16 Aug 2011
PMID: 21676863
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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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Details
- Title
- Arp2/3 complex is bound and activated by two WASP proteins
- Creators
- Shae B. Padrick - Howard Hughes Medical InstituteLynda K. Doolittle - The University of Texas Southwestern Medical CenterChad A. Brautigam - Applied BioPhysics (United States)David S. King - University of California, BerkeleyMichael K. Rosen - Center for Systems Biology
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 108(33), pp E472-E479
- Series
- PNAS Plus
- Publisher
- National Academy of Sciences
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000293895100006
- Scopus ID
- 2-s2.0-80051962603
- Other Identifier
- 991020836602904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology