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First published online November 19, 2008

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Actin' up with tropomodulin

To maintain the highly ordered structure of striated muscle, the polymerisation and depolymerisation of sarcomeric actin filaments must be precisely regulated. The actin-capping protein tropomodulin and the actin-depolymerising proteins ADF/cofilin and AIP1 are thought to regulate sarcomeric actin assembly – but what is the functional relationship between them? On page 3867, Shoichiro Ono and colleagues use the striated body-wall muscle of the nematode worm C. elegans to investigate the in vivo interplay between the worm tropomodulin homologue TMD-1 and other actin regulators. The authors first identify a loss-of-function TMD-1 mutant that has severely disorganised actin filaments in the body-wall muscle. In vitro, they show, TMD-1 antagonises actin depolymerisation by UNC-60B (the worm homologue of ADF/cofilin). Surprisingly, however, knocking down TMD-1 strongly enhances the disorganisation of sarcomeric actin filaments in UNC-60B mutant worms. Moreover, TMD-1 depletion has a similar effect on worms expressing mutant AIP1 or profilin. The authors conclude, therefore, that tropomodulin collaborates with ADF/cofilin, AIP1 and profilin to promote organised actin-filament assembly in sarcomeres. Their data help to decipher how sarcomeric actin is organised in vivo.

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Related articles in JCS:

Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in C. elegans

Sawako Yamashiro, Elisabeth A. Cox, David L. Baillie, Jeff D. Hardin, and Shoichiro Ono
JCS 2008 121: 3867-3877. [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?