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Originally published In Press as doi:10.1074/jbc.M109046200 on February 1, 2002

J. Biol. Chem., Vol. 277, Issue 18, 15241-15251, May 3, 2002
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Alternative Splicing of the Adenylyl Cyclase Stimulatory G-protein Galpha s Is Regulated by SF2/ASF and Heterogeneous Nuclear Ribonucleoprotein A1 (hnRNPA1) and Involves the Use of an Unusual TG 3'-Splice Site*

Alison J. PollardDagger , Adrian R. Krainer§, Stephen C. Robson, and G. Nicholas Europe-Finner

From the Department of Obstetrics and Gynaecology, University of Newcastle upon Tyne, Royal Victoria Infirmary, Richardson Road, Newcastle upon Tyne, NE1 4LP, United Kingdom

The factors involved in regulating alternative splicing of the human adenylyl cyclase stimulatory G-protein Galpha s in different cell types remain undefined. We have designed a Galpha s minigene that retains the signals required for Galpha s alternative splicing in vivo. Employing transient transfection of human myometrial smooth muscle cells and HeLa cells, as well as in vitro splicing assays, we have provided evidence that the antagonistic splicing factors SF2/ASF and hnRNPA1 act as potent regulators of Galpha s isoform expression in these cells. Both SF2/ASF and hnRNPA1 control the selection of competing 5'-splice sites and respectively promote inclusion or skipping of the small cassette-type exon 3 of Galpha s transcripts, resulting in the generation of Galpha s-long and Galpha s-short mRNA isoforms. We have also provided evidence that SF2/ASF and hnRNPA1 play a role in 3'-splice site selection involving the use of a non-canonical TG 3'-splice site preceding exon 4. Using a score-matrix analysis to identify putative exonic enhancer sequences (ESEs), we found multiple high score ESE motifs for SF2/ASF, SC35, and SRp40 in exon 3 of Galpha s. These results suggest that tissue-specific expression of SF2/ASF and hnRNPA1 governs the expression of alternative isoforms of Galpha s in these different cells types.

* This study was funded by a grant from Action Research (S/P/3232).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 44-191-282-4107; Fax: 44-191-222-5066; E-mail: A.J.Pollard@ncl.ac.uk.s.

§ Funded in part by NCI, National Institutes of Health Grant CA13106. Present address: Cold Spring Harbor Laboratory, Box 100, 1 Bungtown Rd., Cold Spring Harbor, NY 11724.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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