Syncoilin is a muscle-specific intermediate filament, first isolated by Newey and colleagues[1] as a binding partner to α-dystrobrevin, as determined by a yeast two-hybrid assay. Later, Poon and colleagues[2] used yeast two-hybrid methods to demonstrate that syncoilin is a binding partner of desmin. 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.
References
^ Newey et al (2001). "Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle". J Biol Chem276 (9): 6645–55. doi:10.1074/jbc.M008305200. PMID 11053421.
^ Poon et al (2002). "Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex". J Biol Chem227 (5): 3433–9. doi:10.1074/jbc.M105273200. PMID 11694502.
^ Brown et al (2005). "Syncoilin upregulation in muscle of patients with neuromuscular disease". Muscle Nerve32 (6): 715–25. doi:10.1002/mus.20431. PMID 16124004.
