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Overview
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Background
The family of SR factors all contain one or more RNA recognition motifs (RRM) and an arginine/serine (RS)-rich domain, are essential for constitutive splicing and also regulate splicing in a concentration-dependent manner by influencing the selection of alternative splice sites. The majority of SR proteins, including SC35 and SRp40, are confined to the nucleus, while SF2/ASF, SRp20, and 9G8 are continuously shuttled between the nucleus and the cytoplasm and contribute to mRNA transport. The activity of SR proteins in regulated splicing is antagonized by members of the hnRNP A/B family of proteins, which induce drastic shifts in the selection of splicing-sites. An additional SR-associated protein, p32, tightly associates with SR factors and preferentially inhibits ASF/SF2 functioning as both a splicing enhancer and splicing repressor protein by preventing the stable interaction of ASF/SF2 and the RNA.
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