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Published online 30 April 2001. doi:10.1083/jcb.153.3.627
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© The Rockefeller University Press, 0021-9525/2001//627 $5.00
The Journal of Cell Biology, Volume 153, Number 3, , 2001 627-634

Original Article

Activation of the Arp2/3 Complex by the Actin Filament Binding Protein Abp1p



Bruce L. Goodea, Avital A. Rodala, Georjana Barnesa, and David G. Drubina

a Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, California 94720-3202
Department of Molecular and Cell Biology, University of California Berkeley, 401 Barker Hall, Berkeley, CA 94720-3202.(510) 643-0062(510) 642-3692

drubin{at}uclink4.berkeley.edu

The actin-related protein (Arp) 2/3 complex plays a central role in assembly of actin networks. Because distinct actin-based structures mediate diverse processes, many proteins are likely to make spatially and temporally regulated interactions with the Arp2/3 complex. We have isolated a new activator, Abp1p, which associates tightly with the yeast Arp2/3 complex. Abp1p contains two acidic sequences (DDW) similar to those found in SCAR/WASp proteins. We demonstrate that mutation of these sequences abolishes Arp2/3 complex activation in vitro. Genetic studies indicate that this activity is important for Abp1p functions in vivo. In contrast to SCAR/WASp proteins, Abp1p binds specifically to actin filaments, not monomers. Actin filament binding is mediated by the ADF/cofilin homology (ADF-H) domain of Abp1p and is required for Arp2/3 complex activation in vitro. We demonstrate that Abp1p recruits Arp2/3 complex to the sides of filaments, suggesting a novel mechanism of activation. Studies in yeast and mammalian cells indicate that Abp1p is involved functionally in endocytosis. Based on these results, we speculate that Abp1p may link Arp2/3-mediated actin assembly to a specific step in endocytosis.

Key Words: actin • yeast • Arp2/3 complex • Abp1 • endocytosis

© 2001 The Rockefeller University Press

Drs. Goode and Rodal contributed equally to this work and should be considered co-first authors.

Dr. Goode's present address is Biology Department and Rosenstiel BMSR Center, Brandeis University, Waltham, MA 02454.

Abbreviations used in this paper: AAP, actin-associated protein; Arp, actin-related protein; HA, hemagglutinin.


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