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

Laura Trinkle-Mulcahy, Paul Ajuh, Alan Prescott, Felix Claverie-Martin, Stanley Cohen, Angus I. Lamond, Philip Cohen

    Research output: Contribution to journalArticlepeer-review

    52 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)157-168
    Number of pages12
    JournalJournal of Cell Science
    Volume112
    Issue number2
    Publication statusPublished - 19 Feb 1999

    Keywords

    • Immunolocalisation
    • NIPP1
    • Protein phosphatase
    • Splicing
    • Targeting subunit

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