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Published online 15 November 2004. doi:10.1083/jcb.200407085
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 4, 639-647
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Article

 The RNA-binding protein SUP-12 controls muscle-specific splicing of the ADF/cofilin pre-mRNA in C. elegans

Akwasi Anyanful1, Kanako Ono1, Robert C. Johnsen2, Hinh Ly1, Victor Jensen2, David L. Baillie2, and Shoichiro Ono1

1 Department of Pathology, Emory University, Atlanta, GA 30322
2 Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6

Correspondence to Shoichiro Ono: sono{at}emory.edu

Tissue-specific alternative pre-mRNA splicing is essential for increasing diversity of functionally different gene products. In Caenorhabditis elegans, UNC-60A and UNC-60B, nonmuscle and muscle isoforms of actin depolymerizing factor (ADF)/cofilin, are expressed by alternative splicing of unc-60 and regulate distinct actin-dependent developmental processes. We report that SUP-12, a member of a new family of RNA recognition motif (RRM) proteins, including SEB-4, regulates muscle-specific splicing of unc-60. In sup-12 mutants, expression of UNC-60B is decreased, whereas UNC-60A is up-regulated in muscle. sup-12 mutations strongly suppress muscle defects in unc-60B mutants by allowing expression of UNC-60A in muscle that can substitute for UNC-60B, thus unmasking their functional redundancy. SUP-12 is expressed in muscle and localized to the nuclei in a speckled pattern. The RRM domain of SUP-12 binds to several sites of the unc-60 pre-mRNA including the UG repeats near the 3'-splice site in the first intron. Our results suggest that SUP-12 is a novel tissue-specific splicing factor and regulates functional redundancy among ADF/cofilin isoforms.

A. Anyanful, K. Ono, and R.C. Johnsen contributed equally to this work.

Abbreviations used in this paper: ADF, actin depolymerizing factor; A/Q-rich, alanine- and glutamine-rich; EMSA, electophoretic mobility shift assay; RRM, RNA recognition motif.


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