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Originally published In Press as doi:10.1074/jbc.M200847200 on March 21, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19855-19860, May 31, 2002
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The Protein Phosphatase-1 Regulator NIPP1 Is Also a Splicing Factor Involved in a Late Step of Spliceosome Assembly*

Monique BeullensDagger and Mathieu Bollen§

From the Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium

NIPP1 is a ubiquitous regulator of protein phosphatase-1 (PP1) and is targeted to the splicing factor storage sites (speckles) in the nucleus by its forkhead-associated domain. We show here that NIPP1 is also a component of the spliceosomes in HeLa cell-splicing extracts and that the interaction with the spliceosomes requires a functional forkhead-associated domain. The in vitro splicing of beta -globin pre-mRNA was not affected by exogenous wild type NIPP1 but was blocked by mutants that lacked residues 225-329. The inhibition by these dominant negative mutants resulted from a block in a late phase of spliceosome assembly, i.e. at the transition between the B-complex and the C-complex. Site-directed mutagenesis furthermore showed that this spliceosomal function of NIPP1 was unrelated to its ability to bind PP1 or RNA. Our data suggest that NIPP1 can function independently as a splicing factor and a phosphatase regulator.

* This work was supported by the Fund for Scientific Research-Flanders Grant G.0374.01 and by a Flemish Concerted Research Action.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 Postdoctoral fellow of the National Fund for Scientific Research-Flanders.

§ To whom correspondence should be addressed: Afdeling Biochemie, Campus Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium. Tel.: 32-16-34-57-01; Fax: 32-16-34-59-95; E-mail: Mathieu.Bollen@med.kuleuven.ac.be.

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