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J. Cell Biol.,
Volume 145, Number 6, June 14, 1999 1251-1264
* Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; Actin interacting protein 1 (Aip1) is a conserved component of the actin cytoskeleton first identified in a two-hybrid screen against yeast actin. Here, we
report that Aip1p also interacts with the ubiquitous actin depolymerizing factor cofilin. A two-hybrid-based approach using cofilin and actin mutants identified residues necessary for the interaction of actin, cofilin, and
Aip1p in an apparent ternary complex. Deletion of the
AIP1 gene is lethal in combination with cofilin mutants
or act1-159, an actin mutation that slows the rate of actin filament disassembly in vivo. Aip1p localizes to cortical actin patches in yeast cells, and this localization is
disrupted by specific actin and cofilin mutations. Further, Aip1p is required to restrict cofilin localization to
cortical patches. Finally, biochemical analyses show that
Aip1p causes net depolymerization of actin filaments
only in the presence of cofilin and that cofilin enhances
binding of Aip1p to actin filaments. We conclude that
Aip1p is a cofilin-associated protein that enhances the
filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches.
State University
of New York Health Science Center, Department of Biochemistry and Molecular Biology, Syracuse, New York 13210; and § Institute of Biotechnology, 00014 University of Helsinki, Finland
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