SYNCOILIN

'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.

Contents

References

External links

References

1. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle, Newey et al, , , J Biol Chem, 2001
2. Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex, Poon et al, , , J Biol Chem, 2002
3. Syncoilin accumulation in two patients with desmin-related myopathy, Howman et al, , , Neuromuscul Disord, 2003
4. Syncoilin upregulation in muscle of patients with neuromuscular disease, Brown et al, , , Muscle Nerve, 2005

External links

★