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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.
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Proteins of the cytoskeleton |
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| Microfilaments |
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| Intermediate filaments |
type 1 and 2 ( Cytokeratin, type I, type II) - type 3 ( Desmin, GFAP, Peripherin, Vimentin) - type 4 ( Internexin, Nestin, Neurofilament, Synemin, Syncoilin) - type 5 ( Lamin A, B)
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| Microtubules |
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| Catenins |
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| Nonhuman |
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| Other |
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Histology: muscle tissue |
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| skeletal muscle/general |
epimysium, fascicle, perimysium, endomysium, muscle fiber ( intrafusal, extrafusal), myofibril
sarcomere (a, i, and h bands; z and m lines), myofilaments (thin filament/actin, thick filament/myosin, elastic filament/titin, nebulin), tropomyosin, troponin (T, C, I)
costamere (dystrophin, α,β-dystrobrevin, syncoilin, synemin/desmuslin, dysbindin, sarcoglycan, dystroglycan, sarcospan), desmin
neuromuscular junction, motor unit, muscle spindle, excitation-contraction coupling, sliding filament mechanism
myoblast, satellite cell, sarcoplasm, sarcolemma, sarcoplasmic reticulum, T-tubule
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| cardiac muscle |
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| smooth muscle |
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