Journal of Cell Science, Vol 112, Issue 2 157-168, Copyright © 1999 by Company of Biologists

JOURNAL ARTICLES

Nuclear organisation of NIPP1, a regulatory subunit of protein phosphatase 1 that associates with pre-mRNA splicing factors

L Trinkle-Mulcahy, P Ajuh, A Prescott, F Claverie-Martin, S Cohen, AI Lamond and P Cohen
Department of Biochemistry, The University, MSI/WTB Complex, Dow Street, Dundee DD1 5EH, Scotland, UK. l.trinklemulcahy@dundee.ac.uk

Protein phosphatase-1 (PP1) is complexed to many proteins that target it to particular subcellular locations and regulate its activity. Here, we show that 'nuclear inhibitor of PP1' (NIPP1), a major nuclear PP1-binding protein, shows a speckled nucleoplasmic distribution where it is colocalised with pre-mRNA splicing factors. One of these factors (Sm) is also shown to be complexed to NIPP1 in nuclear extracts. Immunodepletion of NIPP1 from nuclear extracts, or addition of a 'dominant negative' mutant lacking a functional PP1 binding site, greatly reduces pre-mRNA splicing activity in vitro. These findings implicate the NIPP1-PP1 complex in the control of pre-mRNA splicing.

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