Newey, Sarah E., Howman, Emily V., Ponting, Chris P., Benson, Matthew A., Nawrotzki, Ralph, Loh, Nellie Y., Davies, Kay E. and Blake, Derek J. ORCID: https://orcid.org/0000-0002-5005-4731 2001. Syncoilin, a novel member of the intermediate filament superfamily that interacts with α-dystrobrevin in skeletal muscle. Journal of Biological Chemistry 276 (9) , pp. 6645-6655. 10.1074/jbc.M008305200 |
Abstract
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 α-dystrobrevin, a dystrophin-associated protein whose absence results in neuromuscular junction defects and muscular dystrophy. To gain further insights into the role of α-dystrobrevin in skeletal muscle, we used the yeast two-hybrid system to identify a novel α-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 α-dystrobrevin-1. Expression studies in mammalian cells demonstrate that, while α-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 α-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.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Medicine MRC Centre for Neuropsychiatric Genetics and Genomics (CNGG) |
Subjects: | R Medicine > R Medicine (General) |
Publisher: | American Society for Biochemistry and Molecular Biology |
ISSN: | 0021-9258 |
Last Modified: | 24 Oct 2022 11:46 |
URI: | https://orca.cardiff.ac.uk/id/eprint/49256 |
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