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Published 3 February 2003. doi:10.1083/jcb.200212057
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© The Rockefeller University Press, 0021-9525/2003/2/399 $5.00
The Journal of Cell Biology, Volume 160, Number 3, 399-407

Article

 EPLIN regulates actin dynamics by cross-linking and stabilizing filaments

Raymond S. Maul1,2, Yuhong Song1,2, Kurt J. Amann3, Sachi C. Gerbin1,2, Thomas D. Pollard4 and David D. Chang1,2

1 Department of Medicine, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095
2 Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095
3 Structural Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037
4 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520

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: ddchang{at}mednet.ucla.edu

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.

Key Words: actin stress fibers; lamellipodia; Rac1; actin nucleation; Arp2/3


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