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J. Biol. Chem., Vol. 277, Issue 5, 3433-3439, February 1, 2002
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From the We recently identified a novel
protein called syncoilin, a putative intermediate filament protein that
interacts with The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ251641 and L22550.
Association of Syncoilin and Desmin
LINKING INTERMEDIATE FILAMENT PROTEINS TO THE
DYSTROPHIN-ASSOCIATED PROTEIN COMPLEX*
§¶,
, and§**
Department of Human Anatomy and Genetics and
§ Medical Research Council Functional Genetics Unit,
Department of Human Anatomy and Genetics, University of Oxford, South
Parks Road, Oxford OX13QX, United Kingdom
-dystrobrevin, a member of the dystrophin-associated
protein complex. Syncoilin is found at the neuromuscular junction,
sarcolemma, and Z-lines and is thought to be important for muscle fiber
integrity. Based on the similar protein structure and cellular
localization of syncoilin and desmin, we proposed that these proteins
interact in vivo. The data presented confirm an interaction
between syncoilin and desmin and demonstrate their co-localization in
skeletal muscle. Intriguingly, whereas these proteins interact, COS-7
cell expression studies show that desmin and syncoilin do not assemble
into heterofilaments. Furthermore, fractionation assay and
immunofluorescence study of H2K myoblasts and myotubes suggest that,
unlike typical intermediate filament proteins, syncoilin does not
participate in filament formation with any protein. However, it is
possible that syncoilin is involved in the anchoring of the desmin
intermediate filament network at the sarcolemma and the neuromuscular
junction. This interaction is likely to be important for maintaining
muscle fiber integrity and may also link the dystrophin-associated
protein complex to the cytoskeleton. The dysfunction or absence of
syncoilin may result in the disruption of the intermediate filament
network leading to muscle necrosis. Syncoilin is therefore an
ideal candidate gene for muscular dystrophies and desmin-related myopathies.
*
This work was funded by 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.
A Wellcome prize student. Present address: Cold Spring Harbor
Laboratory, 1 Bungtown Rd., Cold Spring Harbor, NY 11724.
**
To whom correspondence should be addressed: Dept. of Human Anatomy
and Genetics, University of Oxford, South Parks Road, Oxford OX13QX,
United Kingdom. Tel.: 44-1865-272179; Fax: 44-1865-272420; E-mail:
kay.davies@anat.ox.ac.uk.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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