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LocusChr. 1 p35.1-p33

Syncoilin is a muscle-specific intermediate filament, first isolated as a binding partner to α-dystrobrevin, as determined by a yeast two-hybrid assay.[1]

Later, a yeast two-hybrid method was used to demonstrate that syncoilin is a binding partner of desmin.[2] These binding partners suggest that syncoilin acts as a mechanical "linker" between the sarcomere Z-disk (where desmin is localized) and the dystrophin-associated protein complex (where α-dystrobrevin is localized). However, the specific in vivo functions of syncoilin have not yet been determined.

Abnormally high levels of syncoilin have been shown to be a characteristic of neuromuscular wasting diseases such as desminopathy[3] and muscular dystrophy.[4] Therefore, syncoilin is being explored as a promising marker of neuromuscular disease.


  1. Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, Davies KE, Blake DJ (March 2001). "Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle". J. Biol. Chem. 276 (9): 6645–55. doi:10.1074/jbc.M008305200. PMID 11053421.
  2. Poon E, Howman EV, Newey SE, Davies KE (February 2002). "Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex". J. Biol. Chem. 277 (5): 3433–9. doi:10.1074/jbc.M105273200. PMID 11694502.
  3. Howman EV, Sullivan N, Poon EP, Britton JE, Hilton-Jones D, Davies KE (January 2003). "Syncoilin accumulation in two patients with desmin-related myopathy". Neuromuscul. Disord. 13 (1): 42–8. doi:10.1016/S0960-8966(02)00181-5. PMID 12467731.
  4. Brown SC, Torelli S, Ugo I, De Biasia F, Howman EV, Poon E, Britton J, Davies KE, Muntoni F (December 2005). "Syncoilin upregulation in muscle of patients with neuromuscular disease". Muscle Nerve. 32 (6): 715–25. doi:10.1002/mus.20431. PMID 16124004.

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