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First published online 24 July 2008
doi: 10.1242/jcs.034215

Journal of Cell Science 121, 2662-2670 (2008)
Published by The Company of Biologists 2008
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Research Article

Essential role of ADF/cofilin for assembly of contractile actin networks in the C. elegans somatic gonad

Kanako Ono, Sawako Yamashiro and Shoichiro Ono*

Department of Pathology, Emory University, Atlanta, GA 30322, USA

* Author for correspondence (e-mail: sono{at}emory.edu)

Accepted 22 May 2008

The somatic gonad of the nematode Caenorhabditis elegans contains a myoepithelial sheath, which surrounds oocytes and provides contractile forces during ovulation. Contractile apparatuses of the myoepithelial-sheath cells are non-striated and similar to those of smooth muscle. We report the identification of a specific isoform of actin depolymerizing factor (ADF)/cofilin as an essential factor for assembly of contractile actin networks in the gonadal myoepithelial sheath. Two ADF/cofilin isoforms, UNC-60A and UNC-60B, are expressed from the unc-60 gene by alternative splicing. RNA interference of UNC-60A caused disorganization of the actin networks in the myoepithelial sheath. UNC-60B, which is known to function in the body-wall muscle, was not necessary or sufficient for actin organization in the myoepithelial sheath. However, mutant forms of UNC-60B with reduced actin-filament-severing activity rescued the UNC-60A-depletion phenotype. UNC-60A has a much weaker filament-severing activity than UNC-60B, suggesting that an ADF/cofilin with weak severing activity is optimal for assembly of actin networks in the myoepithelial sheath. By contrast, strong actin-filament-severing activity of UNC-60B was required for assembly of striated myofibrils in the body-wall muscle. Our results suggest that an optimal level of actin-filament-severing activity of ADF/cofilin is required for assembly of actin networks in the somatic gonad.

Key words: Actin dynamics, Severing, Contraction, Ovulation, Myoepithelial cells


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