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First published online August 22, 2007

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UNC-87 stabilises actin with a CLIK

Actin filaments are intrinsically dynamic but their stabilisation is essential for actomyosin-based contractility and for maintaining stable cell structures. Tropomyosin stabilises actin filaments by preventing binding of the actin-depolymerising factor cofilin. But, report Shoichiro Ono and colleagues, the nematode protein UNC-87 also antagonises the effects of cofilin (see p. 3022). UNC-87 contains seven calponin-like (CLIK), actin-binding repeats. The authors show that UNC-87 competes with UNC-60B (a muscle-specific form of nematode cofilin) for binding to actin filaments in vitro and inhibits cofilin-dependent actin severing and depolymerisation. In vivo, actin filament stability in the C. elegans body wall muscle is reduced in unc-87 mutants; this disorganised actin phenotype is suppressed in unc-87 unc-60B double mutants. Other results indicate that UNC-87 has a more potent antagonistic effect on cofilin activity than tropomyosin and that the functions of the two actin-stabilising proteins are not identical in vivo. The authors propose, therefore, that tropomyosin and UNC-87 have distinct cellular roles in regulation of actin dynamics.

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UNC-87, a calponin-related protein in C. elegans, antagonizes ADF/cofilin-mediated actin filament dynamics

Sawako Yamashiro, Mario Gimona, and Shoichiro Ono
JCS 2007 120: 3022-3033. [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?