NDLI: NIPP1-mediated Interaction of Protein Phosphatase-1 with CDC5L, a Regulator of Pre-mRNA Splicing and Mitotic Entry

Content Provider	Journal of Biological Chemistry (JBC)
Author	Boudrez, An Beullens, Monique Groenen, Peter Eynde, Aleyde Van Vulsteke, Veerle Jagiello, Izabela Murray, Michael Krainer, Adrian R. Stalmans, Willy Bollen, Mathieu
Abstract	NIPP1 is a regulatory subunit of a species of protein phosphatase-1 (PP1) that co-localizes with splicing factors in nuclear speckles. We report that the N-terminal third of NIPP1 largely consists of a Forkhead-associated (FHA) protein interaction domain, a known phosphopeptide interaction module. A yeast two-hybrid screening revealed an interaction between this domain and a human homolog (CDC5L) of the fission yeast protein cdc5, which is required for G2/M progression and pre-mRNA splicing. CDC5L and NIPP1 co-localized in nuclear speckles in COS-1 cells. Furthermore, an interaction between CDC5L, NIPP1, and PP1 in rat liver nuclear extracts could be demonstrated by co-immunoprecipitation and/or co-purification experiments. The binding of the FHA domain of NIPP1 to CDC5L was dependent on the phosphorylation of CDC5L, e.g.by cyclin E-Cdk2. When expressed in COS-1 or HeLa cells, the FHA domain of NIPP1 did not affect the number of cells in the G2/M transition. However, the FHA domain blocked β-globin pre-mRNA splicing in nuclear extracts. A mutation in the FHA domain that abolished its interaction with CDC5L also canceled its anti-splicing effects. We suggest that NIPP1 either targets CDC5L or an associated protein for dephosphorylation by PP1 or serves as an anchor for both PP1 and CDC5L.
Related Links	http://www.jbc.org/content/275/33/25411.abstract
Ending Page	25417
Starting Page	25411
Page Count	7
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	33
Volume Number	275
DOI	10.1074/jbc.M001676200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2000-08-18
Access Restriction	Open
Subject Keyword	Protein phosphatase-1 (PP1) Enhanced green fluorescent protein (EGFP) Glutathione S-transferase (GST) Hemagglutinin (HA) Phosphate-buffered saline (PBS) Protein phosphatase-2A (PP2A) Catalytic subunit of PP1 (PP1C) Catalytic subunit of PP2A (PP2AC) Heterodimeric complex of NIPP1 and PP1C (PP1NNIPP1) Tris-buffered saline (TBS) Forkhead-associated (FHA) Fluorescence-activated cell sorting (FACS) 4-morpholineethanesulfonic acid (MES) N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine (Tricine) MECHANISMS OF SIGNAL TRANSDUCTION
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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