Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle

S E Newey, E V Howman, C P Ponting, M A Benson, R Nawrotzki, N Y Loh, K E Davies, D J Blake

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 alpha-dystrobrevin, a dystrophin-associated protein whose absence results in neuromuscular junction defects and muscular dystrophy. To gain further insights into the role of alpha-dystrobrevin in skeletal muscle, we used the yeast two-hybrid system to identify a novel alpha-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 alpha-dystrobrevin-1. Expression studies in mammalian cells demonstrate that, while alpha-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 alpha-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.

Original languageEnglish
Pages (from-to)6645-55
Number of pages11
JournalJournal of Biological Chemistry
Volume276
Issue number9
DOIs
Publication statusPublished - 2 Mar 2001

Keywords / Materials (for Non-textual outputs)

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Chromosome Mapping
  • Cytoskeletal Proteins
  • Dystrophin-Associated Proteins
  • Humans
  • Intermediate Filament Proteins
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Muscle, Skeletal
  • Muscular Dystrophies
  • Neuromuscular Junction
  • Transfection

Fingerprint

Dive into the research topics of 'Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle'. Together they form a unique fingerprint.

Cite this