We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure of Arp2/3 complex in its activated state and in actin filament branch junctions.
- Authors
Volkmann, N; Amann, K J; Stoilova-McPhie, S; Egile, C; Winter, D C; Hazelwood, L; Heuser, J E; Li, R; Pollard, T D; Hanein, D
- Abstract
The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.
- Publication
Science (New York, N.Y.), 2001, Vol 293, Issue 5539, p2456
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.1063025