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| LocusSupplementaryData = -p33
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'''Syncoilin''' is a muscle-specific intermediate filament, first isolated as a binding partner to [[DTNA|α-dystrobrevin]], as determined by a [[yeast two-hybrid]] assay.<ref name="pmid11053421">{{cite journal | author = Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, Davies KE, Blake DJ | title = Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle | journal = J. Biol. Chem. | volume = 276 | issue = 9 | pages = 6645–55 | year = 2001 | month = March | pmid = 11053421 | doi = 10.1074/jbc.M008305200 | url = | issn = }}</ref>
'''Syncoilin''' is a muscle-specific intermediate filament, first isolated as a binding partner to [[DTNA|α-dystrobrevin]], as determined by a [[yeast two-hybrid]] assay.<ref name="pmid11053421">{{cite journal | author = Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, Davies KE, Blake DJ | title = Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle | journal = J. Biol. Chem. | volume = 276 | issue = 9 | pages = 6645–55 | year = 2001 | month = March | pmid = 11053421 | doi = 10.1074/jbc.M008305200 | url = }}</ref>


Later, a yeast two-hybrid method was used to demonstrate that syncoilin is a binding partner of [[desmin]].<ref name="pmid11694502">{{cite journal | author = Poon E, Howman EV, Newey SE, Davies KE | title = Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex | journal = J. Biol. Chem. | volume = 277 | issue = 5 | pages = 3433–9 | year = 2002 | month = February | pmid = 11694502 | doi = 10.1074/jbc.M105273200 | url = | issn = }}</ref> 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.
Later, a yeast two-hybrid method was used to demonstrate that syncoilin is a binding partner of [[desmin]].<ref name="pmid11694502">{{cite journal | author = Poon E, Howman EV, Newey SE, Davies KE | title = Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex | journal = J. Biol. Chem. | volume = 277 | issue = 5 | pages = 3433–9 | year = 2002 | month = February | pmid = 11694502 | doi = 10.1074/jbc.M105273200 | url = }}</ref> 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<ref name="pmid12467731">{{cite journal | author = Howman EV, Sullivan N, Poon EP, Britton JE, Hilton-Jones D, Davies KE | title = Syncoilin accumulation in two patients with desmin-related myopathy | journal = Neuromuscul. Disord. | volume = 13 | issue = 1 | pages = 42–8 | year = 2003 | month = January | pmid = 12467731 | doi = | url = http://linkinghub.elsevier.com/retrieve/pii/S0960896602001815 | issn = }}</ref> and [[muscular dystrophy]].<ref name="pmid16124004">{{cite journal | author = Brown SC, Torelli S, Ugo I, De Biasia F, Howman EV, Poon E, Britton J, Davies KE, Muntoni F | title = Syncoilin upregulation in muscle of patients with neuromuscular disease | journal = Muscle Nerve | volume = 32 | issue = 6 | pages = 715–25 | year = 2005 | month = December | pmid = 16124004 | doi = 10.1002/mus.20431 | url = | issn = }}</ref> Therefore, syncoilin is being explored as a promising marker of neuromuscular disease.
Abnormally high levels of syncoilin have been shown to be a characteristic of neuromuscular wasting diseases, such as desminopathy<ref name="pmid12467731">{{cite journal | author = Howman EV, Sullivan N, Poon EP, Britton JE, Hilton-Jones D, Davies KE | title = Syncoilin accumulation in two patients with desmin-related myopathy | journal = Neuromuscul. Disord. | volume = 13 | issue = 1 | pages = 42–8 | year = 2003 | month = January | pmid = 12467731 | doi = 10.1016/S0960-8966(02)00181-5| url = http://linkinghub.elsevier.com/retrieve/pii/S0960896602001815 }}</ref> and [[muscular dystrophy]].<ref name="pmid16124004">{{cite journal | author = Brown SC, Torelli S, Ugo I, De Biasia F, Howman EV, Poon E, Britton J, Davies KE, Muntoni F | title = Syncoilin upregulation in muscle of patients with neuromuscular disease | journal = Muscle Nerve | volume = 32 | issue = 6 | pages = 715–25 | year = 2005 | month = December | pmid = 16124004 | doi = 10.1002/mus.20431 | url = }}</ref> Therefore, syncoilin is being explored as a promising marker of neuromuscular disease.


==References==
==References==

Revision as of 20:39, 19 October 2008

syncoilin
Identifiers
SymbolSYNC1
NCBI gene81493
HGNC28897
OMIM611750
RefSeqNM_030786
UniProtQ9H7C4
Other data
LocusChr. 1 p35.1-p33
Search for
StructuresSwiss-model
DomainsInterPro

Syncoilin is a muscle-specific intermediate filament, first isolated as a binding partner to α-dystrobrevin, as determined by a yeast two-hybrid assay.[1]

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 desminopathy[3] and muscular dystrophy.[4] Therefore, syncoilin is being explored as a promising marker of neuromuscular disease.

References

  1. ^ Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, Davies KE, Blake DJ (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. PMID 11053421. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  2. ^ Poon E, Howman EV, Newey SE, Davies KE (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. PMID 11694502. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  3. ^ Howman EV, Sullivan N, Poon EP, Britton JE, Hilton-Jones D, Davies KE (2003). "Syncoilin accumulation in two patients with desmin-related myopathy". Neuromuscul. Disord. 13 (1): 42–8. doi:10.1016/S0960-8966(02)00181-5. PMID 12467731. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ Brown SC, Torelli S, Ugo I, De Biasia F, Howman EV, Poon E, Britton J, Davies KE, Muntoni F (2005). "Syncoilin upregulation in muscle of patients with neuromuscular disease". Muscle Nerve. 32 (6): 715–25. doi:10.1002/mus.20431. PMID 16124004. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
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