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Originally published In Press as doi:10.1074/jbc.M104005200 on June 20, 2001

J. Biol. Chem., Vol. 276, Issue 34, 32330-32337, August 24, 2001
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Synemin May Function to Directly Link Muscle Cell Intermediate Filaments to Both Myofibrillar Z-lines and Costameres*

Robert M. BellinDagger §, Ted W. HuiattDagger , David R. Critchley, and Richard M. RobsonDagger ||

From the Dagger  Muscle Biology Group, Departments of Biochemistry, Biophysics, and Molecular Biology and of Animal Science, Iowa State University, Ames, Iowa 50011-3260, and  Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom

Synemin is a large intermediate filament (IF) protein that has been identified in all types of muscle cells in association with desmin- and/or vimentin-containing IFs. Our previous studies (Bellin, R. M., Sernett, S. W., Becker, B., Ip, W., Huiatt, T. W., and Robson, R. M. (1999) J. Biol. Chem. 274, 29493-29499) demonstrated that synemin forms heteropolymeric IFs with major IF proteins and contains a binding site for the myofibrillar Z-line protein alpha -actinin. By utilizing blot overlay assays, we show herein that synemin also interacts with the costameric protein vinculin. Furthermore, extensive assays utilizing the Gal4 yeast two-hybrid system demonstrate interactions of synemin with desmin and vimentin and additionally define more precisely the protein subdomains involved in the synemin/alpha -actinin and synemin/vinculin interactions. The C-terminal ~300-amino acid region of synemin binds to the N-terminal head and central rod domains of alpha -actinin and the ~150-amino acid C-terminal tail of vinculin. Overall, these interactions indicate that synemin may anchor IFs to myofibrillar Z-lines via interactions with alpha -actinin and to costameres at the sarcolemma via interactions with vinculin and/or alpha -actinin. These linkages would enable the IFs to directly link all cellular myofibrils and to anchor the peripheral layer of myofibrils to the costameres.

* This research was supported in part by grants from the United States Department of Agriculture, NRICGP Award 99-35206-8676, and American Heart Association, Heartland Affiliate. This is Journal Paper J-19312 of the Iowa Agriculture and Home Economics Experiment Station, Ames, IA 50011, Projects 3597, 3900, and 2127, and supported by Hatch Act and State of Iowa funds.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Children's Hospital, Harvard Medical School, 300 Longwood Ave., Enders-961, Boston, MA 02115.

|| To whom correspondence should be addressed: Muscle Biology Group, 3110 Molecular Biology Bldg., Iowa State University, Ames, IA 50011-3260. Tel.: 515-294-5036; Fax: 515-294-0453; E-mail: rmrobson@iastate.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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