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. |
'''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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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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==References== |
==References== |
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Revision as of 03:16, 13 July 2007
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| 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.
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.[1] An intronic sequence of the synemin β isoform is used as a coding sequence for synemin α.[1]
References
External links
- Synemin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)