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 desminopathy3 and muscular dystrophy.4 Therefore, syncoilin is being explored as a promising marker of neuromuscular disease.
^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. PMID11053421.
^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. PMID11694502.