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Members of the serine/arginine-rich (SR) protein family have multiple functions in the pre-mRNA splicing reaction. In addition to being required for the removal of constitutively spliced introns, SR proteins can function to regulate alternative splicing both in vitro and in vivo (Ge Krainer et al., 1990a; Fu et al., 1992; Zahler et al., 1993a; Caceres et al., 1994; Wang Misteli Misteli et al., 1998) and this undoubtedly underlies some regulated splicing events. However, once in the nucleus and localized to the nascent pre-mRNA, exactly how SR proteins engage the general splicing machinery to recognize specific splice sites is unclear and is an area of intense investigation.
Brenton R. Graveley (Fri,) studied this question.
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