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J. Biol. Chem., Vol. 276, Issue 34, 32330-32337, August 24, 2001
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From the 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
Synemin May Function to Directly Link Muscle Cell Intermediate
Filaments to Both Myofibrillar Z-lines and Costameres*
§,,
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
-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/-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 -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 -actinin and to
costameres at the sarcolemma via interactions with vinculin and/or
-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.
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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