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J. Biol. Chem., Vol. 276, Issue 9, 6645-6655, March 2, 2001
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From the Dystrophin coordinates the assembly of a complex
of structural and signaling proteins that are required for normal
muscle function. A key component of the dystrophin protein complex is The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ251641.
Syncoilin, a Novel Member of the Intermediate Filament
Superfamily That Interacts with
-Dystrobrevin in Skeletal
Muscle*
§¶,,
,,
Department of Human Anatomy and Genetics,
University of Oxford, South Parks Road, Oxford OX1 3QX, United Kingdom
and the § Medical Research Council Functional Genetics Unit,
Department of Human Anatomy and Genetics, University of Oxford, South
Parks Road, Oxford OX1 3QX, United Kingdom
-dystrobrevin, a dystrophin-associated protein whose absence results
in neuromuscular junction defects and muscular dystrophy. To gain
further insights into the role of -dystrobrevin in skeletal muscle,
we used the yeast two-hybrid system to identify a novel -dystrobrevin-binding partner called syncoilin. Syncoilin is a new
member of the intermediate filament superfamily and is highly expressed
in skeletal and cardiac muscle. In normal skeletal muscle, syncoilin is
concentrated at the neuromuscular junction, where it colocalizes and
coimmunoprecipitates with -dystrobrevin-1. Expression studies in
mammalian cells demonstrate that, while -dystrobrevin and syncoilin
associate directly, overexpression of syncoilin does not result in the
self-assembly of intermediate filaments. Finally, unlike many
components of the dystrophin protein complex, we show that syncoilin
expression is up-regulated in dystrophin-deficient muscle. These data
suggest that -dystrobrevin provides a link between the dystrophin
protein complex and the intermediate filament network at the
neuromuscular junction, which may be important for the maintenance and
maturation of the synapse.
*
This work was funded by the Wellcome Trust and the Medical
Research Council.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: Dept. of Anatomy and Cellular Neurobiology,
University of Ulm, Albert Einstein Allee 11, 89069 Ulm, Germany.
**
To whom correspondence should be addressed: MRC Functional
Genetics Unit, Dept. of Human Anatomy and Genetics, University of
Oxford, South Parks Rd., Oxford, OX1 3QX, United Kingdom. Tel.: 44-1865-272179; Fax: 44-1865-272-427; E-mail:
kay.davies@anat.ox.ac.uk.
A Wellcome Trust Senior Fellow.
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