Synemin: Difference between revisions
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'''Synemin''', also called '''desmuslin''', is an [[intermediate filament]] (IF) and, like other IFs, primarily functions to integrate mechanical stress and maintain structural integrity in eukaryotic cells. While it has been observed in a variety of cell types, it is has been best studied in the [[sarcomere]] of skeletal myocytes. It localizes at the Z-disk and has been shown to bind to both α-actinin and [[desmin]] to act as a mechanical linker in transmitting [[force]] laterally throughout the tissue, especially between the contractile [[myofibril]]s and extracellular matrix. |
'''Synemin''', also called '''desmuslin''', is an [[intermediate filament]] (IF) and, like other IFs, primarily functions to integrate mechanical stress and maintain structural integrity in eukaryotic cells. While it has been observed in a variety of cell types, it is has been best studied in the [[sarcomere]] of skeletal myocytes. It localizes at the Z-disk and has been shown to bind to both α-actinin and [[desmin]] to act as a mechanical linker in transmitting [[force]] laterally throughout the tissue, especially between the contractile [[myofibril]]s and extracellular matrix. |
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Synemin has properties very similar to the intermediate filament [[syncoilin]]. In particular, it binds to α-dystrobrevin in the [[dystrophin]]-associated protein complex to act as a mechanical "linker" between the myofibrillar network and the cell membrane.<ref name="mizuno">{{cite journal |author=Mizuno et al |title=Desmuslin, an intermediate filament protein that interacts with alpha-dystrobrevin and desmin |journal=Proc Natl Acad Sci USA |volume=98 |issue=11 |pages=6156-61 |year=2001 |pmid=11353857 }}</ref> |
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Two [[splice variant]] isoforms of synemin exist, α and β. Both isoforms have a very short N-terminal domain of 10 amino acids and a long C-terminal domain consisting of 1243 amino acids for the α isoform and 931 amino acids for the β isoform.<ref name="titeux">{{cite journal |author=Titeux et al |title=Human synemin gene generates splice variants encoding two distinct intermediate filament proteins |journal=Eur J Biochem |volume=268 |issue=24 |pages=6435-49 |year=2001 |pmid=11737198}}</ref> An intronic sequence of the synemin β isoform is used as a coding sequence for synemin α.<ref name="titeux"/> |
Two [[splice variant]] isoforms of synemin exist, α and β. Both isoforms have a very short N-terminal domain of 10 amino acids and a long C-terminal domain consisting of 1243 amino acids for the α isoform and 931 amino acids for the β isoform.<ref name="titeux">{{cite journal |author=Titeux et al |title=Human synemin gene generates splice variants encoding two distinct intermediate filament proteins |journal=Eur J Biochem |volume=268 |issue=24 |pages=6435-49 |year=2001 |pmid=11737198}}</ref> An intronic sequence of the synemin β isoform is used as a coding sequence for synemin α.<ref name="titeux"/> |
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Revision as of 03:23, 13 July 2007
 | This cell biology article is a stub. You can help Wikipedia by expanding it. |
 | This protein-related article is a stub. You can help Wikipedia by expanding it. |
| synemin, desmuslin | |
|---|---|
| Identifiers | |
| Symbol | DMN |
| NCBI gene | 23336 |
| HGNC | 14466 |
| Other data | |
| Locus | Chr. 15 q26.3 |
Synemin, also called desmuslin, is an intermediate filament (IF) and, like other IFs, primarily functions to integrate mechanical stress and maintain structural integrity in eukaryotic cells. While it has been observed in a variety of cell types, it is has been best studied in the sarcomere of skeletal myocytes. It localizes at the Z-disk and has been shown to bind to both α-actinin and desmin to act as a mechanical linker in transmitting force laterally throughout the tissue, especially between the contractile myofibrils and extracellular matrix.
Synemin has properties very similar to the intermediate filament syncoilin. In particular, it binds to α-dystrobrevin in the dystrophin-associated protein complex to act as a mechanical "linker" between the myofibrillar network and the cell membrane.[1]
Two splice variant isoforms of synemin exist, α and β. Both isoforms have a very short N-terminal domain of 10 amino acids and a long C-terminal domain consisting of 1243 amino acids for the α isoform and 931 amino acids for the β isoform.[2] An intronic sequence of the synemin β isoform is used as a coding sequence for synemin α.[2]
References
- ^ Mizuno; et al. (2001). "Desmuslin, an intermediate filament protein that interacts with alpha-dystrobrevin and desmin". Proc Natl Acad Sci USA. 98 (11): 6156–61. PMID 11353857.
{{cite journal}}: Explicit use of et al. in:|author=(help) - ^ a b Titeux; et al. (2001). "Human synemin gene generates splice variants encoding two distinct intermediate filament proteins". Eur J Biochem. 268 (24): 6435–49. PMID 11737198.
{{cite journal}}: Explicit use of et al. in:|author=(help)
External links
- Synemin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)