Syncoilin

Syncoilin is a muscle-specific intermediate filament, first isolated by Newey et al (2001) as a binding partner to α-dystrobrevin, as determined by a yeast two-hybrid assay. Later, Poon et al (2002) 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).

Abnormally high levels of syncoilin have been shown to be a characteristic of neuromuscular wasting diseases, such as desminopathy (Howman et al, 2003) and muscular dystrophy (Brown et al, 2005).

References

1. Brown et al, "Syncoilin upregulation in muscle of patients with neuromuscular disease." Muscle Nerve. 2005 Dec;32(6):715-25.

2. Howman et al, "Syncoilin accumulation in two patients with desmin-related myopathy." Neuromuscul Disord. 2003 Jan;13(1):42-8.

3. Newey et al, "Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle." J Biol Chem. 2001 Mar 2;276(9):6645-55.

4. Poon et al, "Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex." J Biol Chem. 2002 Feb 1;277(5):3433-9.