Synemin
SYNM | |||
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Identifiers | |||
Gene ontology | |||
Molecular function | |||
Cellular component | |||
Biological process | |||
Sources:Amigo / QuickGO |
Ensembl | |||||||||
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UniProt | |||||||||
RefSeq (mRNA) | |||||||||
RefSeq (protein) | |||||||||
Location (UCSC) | Chr 15: 99.1 – 99.14 Mb | Chr 7: 67.38 – 67.41 Mb | |||||||
PubMed search | [3] | [4] |
View/Edit Human | View/Edit Mouse |
Synemin, also known as desmuslin, is a
cytoskeletal proteins that confer resistance to mechanical stress and are encoded by a dispersed multigene family. This protein has been found to form a linkage between desmin, which is a subunit of the IF network, and the extracellular matrix
, and provides an important structural support in muscle.
Function
Synemin is an
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 contributes to linkage between costameres and the contractile apparatus in skeletal muscle of synemin null animals.[6] Synemin plays an important regulatory role in the heart and the consequences of its absence are profound.[7]
Properties
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.[8]
Splice variants
Three
splice variant isoforms of synemin exist, α and β and L. 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.[9] An intronic sequence of the synemin β isoform is used as a coding sequence for synemin α.[9][10]
Cancer
SYNM gene has been observed progressively downregulated in
Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy.[11] For this reason, SYNM is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.[11]
History
The origin of the synemin/desmuslin naming convention is quite complex. In 1980, synemin was first identified in
coimmunoprecipitation assays could not detect an interaction between human desmuslin and α-actinin.[8] In 2001, Titeux and colleagues reported the cloning of the α and β splice-varying isoforms of human synemin and showed that β-synemin was identical to desmuslin.[9] In 2014 was reported the first synemin -/- null animal.[6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000182253 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030554 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: Synemin, intermediate filament protein".
- ^ PMID 25567810.
- PMID 29247678.
- ^ PMID 11353857.
- ^ PMID 11737198.
- ISBN 978-0-12-803491-0.[page needed]
- ^ S2CID 24986454.
- S2CID 24349058.
External links
- Synemin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.