J. Lipid Res.
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Papers In Press, published online ahead of print February 27, 2006
J. Lipid Res., doi:10.1194/jlr.C600003-JLR200
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Submitted on January 19, 2006
Revised on February 14, 2006
Accepted on February 26, 2006

SRp30a (ASF/SF2) regulates the alternative splicing of caspase-9 pre-mRNA and is required for ceramide-responsiveness

Autumn Massiello and Charles E. Chalfant

Biochemistry, Virginia Commonwealth University, Richmond, VA 23298-0614

Corresponding Author: cechalfant{at}vcu.edu

Two splice variants are derived from the caspase-9 gene, pro-apoptotic caspase-9a and anti-apoptotic caspase-9b, by either the inclusion or exclusion of an exon 3, 4, 5, and 6 cassette. Previous studies by our laboratory have shown that the alternative splicing of caspase-9 and the phospho-status of SR proteins, a conserved family of splicing factors, are regulated by chemotherapy and ceramide via the action of protein phophatase-1 (PP1). In this study, a link between ceramide, SR proteins, and the alternative splicing of caspase-9 was established. The downregulation of SRp30a in A549 cells by RNA interference technology resulted in an increase in the caspase-9b splice variant with a concomitant decrease in the caspase-9a splice variant, thereby significantly decreasing the caspase-9a/caspase-9b ratio from 1.67 ± 0.11 to 0.56 ± 0.08, * p < 0.005. The specific downregulation of SRp30a also inhibited the ability of exogenous ceramide treatment to induce the inclusion of the exon 3, 4, 5, and 6 cassette. Therefore, we have identified SRp30a as an RNA trans-acting factor that functions as a major regulator of caspase-9 pre-mRNA processing, and is required for ceramide to mediate the alternative splicing of caspase-9.


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