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

Laura TrinkleMulcahy | Zendy; Paul Ajuh | Zendy; Alan R. Prescott | Zendy; Félix Claverie-Martı́n | Zendy; Stanley N. Cohen | Zendy; Angus I. Lamond | Zendy; Philip Cohen | Zendy

Open Access

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

Author(s) -

Laura TrinkleMulcahy,

Paul Ajuh,

Alan R. Prescott,

Félix Claverie-Martı́n,

Stanley N. Cohen,

Angus I. Lamond,

Philip Cohen

Publication year - 1999

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.112.2.157

Subject(s) - biology , rna splicing , protein phosphatase 1 , messenger rna , precursor mrna , nuclear protein , phosphatase , alternative splicing , rna binding protein , microbiology and biotechnology , protein subunit , cell nucleus , splicing factor , phosphorylation , genetics , gene , rna , cytoplasm , transcription factor

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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