Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing.

Molecular and Cellular Biology
W J Zhang, J Y Wu

Abstract

Previous studies have shown that protein-protein interactions among splicing factors may play an important role in pre-mRNA splicing. We report here identification and functional characterization of a new splicing factor, Sip1 (SC35-interacting protein 1). Sip1 was initially identified by virtue of its interaction with SC35, a splicing factor of the SR family. Sip1 interacts with not only several SR proteins but also with U1-70K and U2AF65, proteins associated with 5' and 3' splice sites, respectively. The predicted Sip1 sequence contains an arginine-serine-rich (RS) domain but does not have any known RNA-binding motifs, indicating that it is not a member of the SR family. Sip1 also contains a region with weak sequence similarity to the Drosophila splicing regulator suppressor of white apricot (SWAP). An essential role for Sip1 in pre-mRNA splicing was suggested by the observation that anti-Sip1 antibodies depleted splicing activity from HeLa nuclear extract. Purified recombinant Sip1 protein, but not other RS domain-containing proteins such as SC35, ASF/SF2, and U2AF65, restored the splicing activity of the Sip1-immunodepleted extract. Addition of U2AF65 protein further enhanced the splicing reconstitution by the Sip1 protein....Continue Reading

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Citations

Apr 25, 2006·Biochemical and Biophysical Research Communications·Theoni LeoutsakouAndreas Scorilas
May 21, 2014·Nature Reviews. Neurology·Hao DengJoseph Jankovic
Dec 14, 1999·The Journal of Biological Chemistry·M Golovkin, A S Reddy
Jun 27, 2001·The Journal of Biological Chemistry·S AwasthiS W Ruby
Mar 31, 2005·Molecular and Cellular Biology·Demian CazallaJavier F Cáceres

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