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J. Biol. Chem., Vol. 278, Issue 46, 46094-46106, November 14, 2003

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F-actin and Myosin II Binding Domains in Supervillin^*

Yu Chen¶, Norio Takizawa¶, Jessica L. Crowley, Sang W. Oh, Cheryl L. Gatto, Taketoshi Kambara||, Osamu Sato||, Xiang-dong Li||, Mitsuo Ikebe||, and Elizabeth J. Luna**

From the Department of Cell Biology, the ^||Department of Physiology, and Program in Cell Dynamics, the University of Massachusetts Medical School, Worcester, Massachusetts 01605

Detergent-resistant membranes contain signaling and integral membrane proteins that organize cholesterol-rich domains called lipid rafts. A subset of these detergent-resistant membranes (DRM-H) exhibits a higher buoyant density (1.16 g/ml) because of association with membrane skeleton proteins, including actin, myosin II, myosin 1G, fodrin, and an actin- and membrane-binding protein called supervillin (Nebl, T., Pestonjamasp, K. N., Leszyk, J. D., Crowley, J. L., Oh, S. W., and Luna, E. J. (2002) J. Biol. Chem. 277, 43399-43409). To characterize interactions among DRM-H cytoskeletal proteins, we investigated the binding partners of the novel supervillin N terminus, specifically amino acids 1-830. We find that the supervillin N terminus binds directly to myosin II, as well as to F-actin. Three F-actin-binding sites were mapped to sequences within amino acids 280-342, 344-422, and 700-830. Sequences with combinations of these sites promote F-actin cross-linking and/or bundling. Supervillin amino acids 1-174 specifically interact with the S2 domain in chicken gizzard myosin and nonmuscle myosin IIA (MYH-9) but exhibit little binding to skeletal muscle myosin II. Direct or indirect binding to filamin also was observed. Overexpression of supervillin amino acids 1-174 in COS7 cells disrupted the localization of myosin IIB without obviously affecting actin filaments. Taken together, these results suggest that supervillin may mediate actin and myosin II filament organization at cholesterol-rich membrane domains.

Received for publication, May 20, 2003 , and in revised form, August 4, 2003.

^* This work was supported by National Institutes of Health Research Grants GM33048 (to E. J. L.), GM55834, and AR41653 (to M. I.) and by the Muscular Dystrophy Association (to E. J. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Table II.

^¶ Both authors contributed equally to this work.

^** To whom correspondence should be addressed: Dept. of Cell Biology, Biotech 4, Ste. 306, 377 Plantation St., Worcester, MA 01605. Tel.: 508-856-8661; Fax: 508-856-8774; E-mail: Elizabeth.Luna{at}umassmed.edu.

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