Analysis of SRrp86-regulated alternative splicing: control of c-Jun and IκBβ activity.

Solis AS, Patton JG
RNA Biol. 2010 7 (4): 486-94

PMID: 20400856 · PMCID: PMC3070911 · DOI:10.4161/rna.7.4.11567

Previous work led to the hypothesis that SRrp86, a related member of the SR protein superfamily, can interact with and modulate the activity of other SR proteins. Here, we sought to test this hypothesis by examining the effect of changing SRrp86 concentrations on overall alternative splicing patterns. SpliceArrays were used to examine 9,854 splicing events in wild-type cells, cells overexpressing SRrp86, and cells treated with siRNAs to knockdown SRrp86. From among the 500 splicing events exhibiting altered splicing under these conditions, the splicing of c-Jun and IκBβ were validated as being regulated by SRrp86 resulting in altered regulation of their downstream targets. In both cases, functionally distinct isoforms were generated that demonstrate the role SRrp86 plays in controlling alternative splicing.

MeSH Terms (14)

Alternative Splicing Animals Cell Line, Tumor HeLa Cells Humans I-kappa B Proteins Microarray Analysis NF-kappa B Nuclear Proteins Proto-Oncogene Proteins c-jun Rats RNA-Binding Proteins RNA Splicing Serine-Arginine Splicing Factors

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