Myotilin

Myotilin, Eng. also titin immunoglobulin domain protein, TTID for short, 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 ). Myotilin is formed in humans in the sarcolemma of skeletal muscles, the heart muscles, bone marrow and the thyroid gland.

Design and function

The exact function of myotilin is not known yet. Myotilin has three immunoglobulin-like (Ig -like) domains at the carboxyl terminus. About these domains can form antiparallel dimers per 2 myotilin molecules. Myotilin also has two binding sites for other proteins, alpha -actinin, filamin, and C. Alpha -actinin is one of the main components of the Z-line of the sarcomere in muscle and is used, inter alia, the combination of actin filaments ( "cross -linking ").

It is also believed that in the formation of myotilin sarcomeres plays an important role ( Myofibrillinogenese ). Over-expression of myotilin led to abnormally thick muscle fibers in vitro experiments.

Medical importance

Mutations in MYOT gene can lead to three allelic muscle diseases collectively known as Myotilinopathien.

Swell

  • D. Selcen, A. G. Engel: myofibrillar myopathies. In: Handbook of clinical neurology / edited by PJ Vinken and G.W. Bruyn Volume 101, 2011, pp. 143-154, ISSN 0072-9752. doi: 10.1016/B978-0-08-045031-5.00011-6. PMID 21,496,631th (Review).
Protein isoform Human Genome Organisation Dimer (chemistry) Digital Object Identifier
589302
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