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syncoilin
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| Identifiers | |
| Symbol | SYNC1 |
| Entrez | 81493 |
| HUGO | 28897 |
| UniProt | Q9H7C4 |
| Other data | |
| Locus | Chr. 1 p35.1-p33 |
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 Chem 276 (9): 6645–55. doi:. PMID 11053421.
- ^ Poon et al (2002). "Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex". J Biol Chem 227 (5): 3433–9. doi:. PMID 11694502.
- ^ Howman et al (2003). "Syncoilin accumulation in two patients with desmin-related myopathy". Neuromuscul Disord 13 (1): 42–8. doi:. PMID 12467731.
- ^ Brown et al (2005). "Syncoilin upregulation in muscle of patients with neuromuscular disease". Muscle Nerve 32 (6): 715–25. doi:. PMID 16124004.
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Wikipedia content modification information:
- This page was last modified on 7 July 2008, at 21:35.
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