Aip1p Interacts with Cofilin to Disassemble Actin Filaments

Rodal, Avital A.; Tetreault, Jonathan W.; Lappalainen, Pekka; Drubin, David G.; Amberg, David C.

doi:10.1083/jcb.145.6.1251

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Article| June 14 1999

Aip1p Interacts with Cofilin to Disassemble Actin Filaments

Avital A. Rodal,

Avital A. Rodal

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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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Jonathan W. Tetreault,

Jonathan W. Tetreault

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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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Pekka Lappalainen,

Pekka Lappalainen

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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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David G. Drubin,

David G. Drubin

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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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David C. Amberg

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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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Author and Article Information

Avital A. Rodal

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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

Jonathan W. Tetreault

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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

Pekka Lappalainen

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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

David G. Drubin

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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

David C. Amberg

*Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720; †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

Address correspondence to David C. Amberg, State University of New York Health Science Center, Department of Biochemistry and Molecular Biology, Syracuse, NY 13210. Tel.: (315) 464-8727. Fax: (315) 464-8750. E-mail: [email protected]

Research in D.C. Amberg's laboratory was supported by National Institutes of Health (NIH) grant GM56189. Research in D.G. Drubin's laboratory was supported by NIH grant GM42759 and A.A. Rodal was supported by a Howard Hughes Medical Institute Predoctoral Fellowship.

Received: November 12 1998

Revision Received: May 05 1999

Online ISSN: 1540-8140

Print ISSN: 0021-9525

1999

J Cell Biol (1999) 145 (6): 1251–1264.

https://doi.org/10.1083/jcb.145.6.1251

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.

1999

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