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Originally published in Science Express on 30 August 2001
Science 28 September 2001: Vol. 293. no. 5539, pp. 2456 - 2459
DOI: 10.1126/science.1063025
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Reports
Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions
Niels Volkmann,1
Kurt J. Amann,2
Svetla Stoilova-McPhie,1
Coumaran Egile,3
Dirk C. Winter,3
Larnele Hazelwood,1
John E. Heuser,4
Rong Li,3
Thomas D. Pollard,2
Dorit Hanein1*
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.
1 The Burnham Institute, La Jolla, CA 92037, USA.
2 Structural Biology Laboratory, Salk Institute
for Biological Studies, La Jolla, CA 92037, USA.
3 Department of Cell Biology, Harvard Medical
School, Boston, MA 02115, USA.
4 Department of Cell
Biology, Washington University, School of Medicine, St. Louis, MO
63110, USA.
*
To whom correspondence should be addressed. E-mail:
dorit{at}burnham.org
Read the Full Text
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