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First published online October 12, 2006

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Sarcomere formation – a titin-ic task

Titin is a massive filamentous protein expressed in cardiac and striated muscle. It functions as a `molecular ruler' that binds numerous signalling/structural proteins and stretches 1 µM from the Z-disc to the M-band of the muscle sarcomere. On p. 4322, Michelle Peckham and co-workers expose its critical role in the development of muscle fibres. To do this they have created embryonic stem (ES) cells in which titin is mutated and monitored their differentiation to form cardiomyocytes. They find that cells in which both alleles are mutated fail to differentiate properly. The cells do not beat; moreover, the striations characteristic of muscle do not form, and proteins such as myosin and -actinin instead localize to disorganized filaments or primitive dot-like structures. Fully functional titin thus seems to be essential for myofibrillogenesis. The mutant protein expressed in the cells lacks the M-band region that contains the titin kinase (TK) domain and binding sites for various M-band proteins. Surprisingly, however, Z-disk maturation is also defective in the cells. Communication between the M-band region of titin and events at the other end of the sarcomere must therefore be important during myofibrillogenesis.

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Targeted homozygous deletion of M-band titin in cardiomyocytes prevents sarcomere formation

Hanny Musa, Stephen Meek, Mathias Gautel, Dianna Peddie, Andrew J. H. Smith, and Michelle Peckham
JCS 2006 119: 4322-4331. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?