EPLIN regulates actin dynamics by cross-linking and stabilizing filaments

Maul , Raymond S.; Song , Yuhong; Amann , Kurt J.; Gerbin , Sachi C.; Pollard , Thomas D.; Chang , David D.

doi:10.1083/jcb.200212057

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Article| February 03 2003

EPLIN regulates actin dynamics by cross-linking and stabilizing filaments

Raymond S. Maul,

Raymond S. Maul

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

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Yuhong Song,

Yuhong Song

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

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Kurt J. Amann,

Kurt J. Amann

3Structural Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037

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Sachi C. Gerbin,

Sachi C. Gerbin

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

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Thomas D. Pollard,

Thomas D. Pollard

4Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520

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David D. Chang

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

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Author and Article Information

Raymond S. Maul

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

Yuhong Song

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

Kurt J. Amann

3Structural Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037

Sachi C. Gerbin

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

Thomas D. Pollard

4Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520

David D. Chang

1Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

2Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095

Address correspondence to David D. Chang, University of California, Los Angeles, School of Medicine, Division of Heme-Onc, Factor 11-934, 10833 Le Conte Ave., Los Angeles, CA 90095-1678. Tel.: (310) 825-9759. Fax: (310) 825-6192. E-mail: [email protected]

*

Abbreviation used in this paper: EPLIN, epithelial protein lost in neoplasm.

Received: December 09 2002

Revision Received: December 23 2002

Accepted: December 23 2002

Online ISSN: 1540-8140

Print ISSN: 0021-9525

The Rockefeller University Press

2003

J Cell Biol (2003) 160 (3): 399–407.

https://doi.org/10.1083/jcb.200212057

Epithelial protein lost in neoplasm (EPLIN) is a cytoskeleton-associated protein encoded by a gene that is down-regulated in transformed cells. EPLIN increases the number and size of actin stress fibers and inhibits membrane ruffling induced by Rac. EPLIN has at least two actin binding sites. Purified recombinant EPLIN inhibits actin filament depolymerization and cross-links filaments in bundles. EPLIN does not affect the kinetics of spontaneous actin polymerization or elongation at the barbed end, but inhibits branching nucleation of actin filaments by Arp2/3 complex. Side binding activity may stabilize filaments and account for the inhibition of nucleation mediated by Arp2/3 complex. We propose that EPLIN promotes the formation of stable actin filament structures such as stress fibers at the expense of more dynamic actin filament structures such as membrane ruffles. Reduced expression of EPLIN may contribute to the motility of invasive tumor cells.

The Rockefeller University Press

2003

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