RNA



REVIEW

Sorting out the complexity of SR protein functions


BRENTON R.  GRAVELEY a1c1
a1 Department of Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, Connecticut 06030, USA

Abstract

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 & Manley, 1990; Krainer et al., 1990a; Fu et al., 1992; Zahler et al., 1993a; Caceres et al., 1994; Wang & Manley, 1995). In the cell, SR proteins migrate from speckles—subnuclear domains that may function as storage sites for certain splicing factors—to sites of active transcription (Misteli et al., 1997; Misteli & Spector, 1999) and some SR proteins have been found to shuttle in and out of the nucleus (Caceres et al., 1998). The subcellular localization of SR proteins can be modulated by phosphorylation (Misteli & Spector, 1998; 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.

(Received May 11 2000)
(Revised June 9 2000)
(Accepted June 23 2000)


Correspondence:
c1 Reprint requests to: Brenton R. Graveley, Department of Genetics and Developmental Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06030, USA; e-mail: graveley@neuron.uchc.edu.