Myotilin
| Myotilin | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 498 AA, 57 kDa | |
| Secondary to quaternary structure | Homodimer | |
| Isoforms | 2 | |
| Identifier | ||
| Gene name | MYOT | |
| External IDs | ||
| Occurrence | ||
| Parent taxon | Terrestrial vertebrates | |
Myotilin , engl. also Titin immunoglobulin domain protein , shortly TTID , is a protein in mammals and some reptiles . In humans, it is encoded by the myotilin gene (MYOT) and is located on the long arm of chromosome 5 (5q31.2). In humans, myotilin is formed in the sarcolemma of the skeletal muscles , the heart muscles , the bone marrow and the thyroid gland .
Layout and function
The exact function of myotilin is not yet known. Myotilin has two immunoglobulin-like (Ig-like) domains at the carboxy terminus . Via these domains, 2 myotilin molecules can each form antiparallel dimers . Myotilin also has binding sites for two additional proteins, alpha-actinin and Filamin C . Alpha-actinin is one of the main components of the Z-disk of the sarcomere in the muscle and is used, among other things, to connect actin filaments ("cross-linking").
It is also assumed that myotilin plays an important role in the formation of sarcomeres (myofibrillinogenesis). Overexpression of myotilin resulted in abnormally thick muscle fibers in in vitro experiments.
Medical importance
Mutations in the MYOT gene can lead to three allelic muscle diseases collectively referred to as myotilinopathies .
swell
- D. Selcen, AG Engel: Myofibrillar myopathies. In: Handbook of clinical neurology / edited by PJ Vinken and GW Bruyn Volume 101, 2011, pp. 143-154, ISSN 0072-9752 . doi : 10.1016 / B978-0-08-045031-5.00011-6 . PMID 21496631 . (Review).
Individual evidence
- ↑ D. Selcen, AG Engel: Myofibrillar myopathies. In: Handbook of clinical neurology / edited by PJ Vinken and GW Bruyn Volume 101, 2011, pp. 143-154, ISSN 0072-9752 . doi : 10.1016 / B978-0-08-045031-5.00011-6 . PMID 21496631 . (Review).
- ↑ Orthologist at OMA
- ↑ UniProt Q9UBF9
- ↑ L. Broglio, M. Tentorio et al. a .: Limb-girdle muscular dystrophy-associated protein diseases. In: The neurologist. Volume 16, Number 6, November 2010, pp. 340-352, ISSN 1074-7931 . doi: 10.1097 / NRL.0b013e3181d35b39 . PMID 21150381 . (Review).
further reading
- J. Wang, DK Dube et al. a .: Myotilin dynamics in cardiac and skeletal muscle cells. In: Cytoskeleton (Hoboken, NJ). [electronic publication before printing] October 2011, ISSN 1949-3592 . doi : 10.1002 / cm.20542 . PMID 22021208 .
- P. von Nandelstadh, R. Soliymani u. a .: Analysis of myotilin turnover provides mechanistic insight into the role of myotilinopathy-causing mutations. In: The Biochemical journal . Volume 436, Number 1, May 2011, pp. 113-121, ISSN 1470-8728 . doi : 10.1042 / BJ20101672 . PMID 21361873 .
- J. Ochala, O. Carpén, L. Larsson: Maintenance of muscle mass, fiber size, and contractile function in mice lacking the Z-disc protein myotilin. In: Upsala journal of medical sciences. Volume 114, Number 4, 2009, pp. 235-241, ISSN 2000-1967 . doi : 10.3109 / 03009730903276399 . PMID 19878039 . PMC 2852774 (free full text).
- L. Carlsson, JG Yu et al. a .: Myotilin: a prominent marker of myofibrillar remodeling. In: Neuromuscular disorders: NMD. Volume 17, Number 1, January 2007, pp. 61-68, ISSN 0960-8966 . doi : 10.1016 / j.nmd.2006.09.007 . PMID 17056257 .