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First published online May 20, 2008

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Making sense of the M-band

To help maintain the highly ordered sarcomeric structure of myofibrils, the myosin-containing contractile filaments of striated muscle are crosslinked with other proteins at the M-band region of the sarcomere. The proteins titin and myomesin are known to interact with myosin filaments at the M-band, but the role of other M-band-localised proteins – such as the giant protein obscurin – is less well understood. On page 1841, Mathias Gautel and colleagues explore the interprotein interactions of obscurin and its newly discovered homologue obscurin-like 1 (Obsl1). Using a yeast two-hybrid system, the authors show that obscurin and Obsl1 both interact with myomesin and with the extreme C-terminal M10 domain of titin; moreover, obscurin can form a ternary complex with titin and myomesin. The M-band localisation of obscurin is disrupted when the titin- or myomesin-binding domains of obscurin (or the corresponding domains of myomesin and titin) are overexpressed, or when myomesin is knocked down. Importantly, muscle-disease-associated mutations in the titin M10 domain weaken the interaction between titin and obscurin or Obsl1. Based on their data, the authors propose a revised model of protein interactions at the M-band.

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Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band – implications for hereditary myopathies

Atsushi Fukuzawa, Stephan Lange, Mark Holt, Anna Vihola, Virginie Carmignac, Ana Ferreiro, Bjarne Udd, and Mathias Gautel
JCS 2008 121: 1841-1851. [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?