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Interaction of the Protein Phosphatase-1 Regulator Nipp1 With Pre-Mrna Splicing Factors

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Published by Leuven Univ Pr .
Written in English

Subjects:

  • Physiology,
  • Proteins,
  • Life Sciences - Biochemistry,
  • Science,
  • Science/Mathematics

Book details:

Edition Notes

SeriesActa Biomedica Lovaniensia, 257
The Physical Object
FormatPaperback
Number of Pages116
ID Numbers
Open LibraryOL12845997M
ISBN 109058672182
ISBN 109789058672186
OCLC/WorldCa49867965

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  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 by:   Abstract. The nuclear protein NIPP1 (n uclear i nhibitor of p rotein Ser/Thr p hosphatase-1) interacts with the splicing factors SAP and CDC5L and is involved in a late step of spliceosome addition, NIPP1 is an interactor of protein phosphatase-1 and a COOH-terminal NIPP1 fragment displays an RNase E like endoribonuclease activity. Nuclear inhibitor of protein phosphatase 1 is an enzyme that in humans is encoded by the PPP1R8 gene.. This gene, through alternative splicing, encodes three different of the protein isoforms encoded by this gene are specific inhibitors of type 1 serine/threonine protein phosphatases and can bind but not cleave s: PPP1R8, ARD-1, ARD1, NIPP-1, . Rent or Buy Interaction of the Protein Phosphatase-1 Regulator Nipp1 With Pre-Mrna Splicing Factors - by Boudrez, an for as low as $ at Voted #1 site for Buying Textbooks.

Up to 90% off Textbooks at Amazon Canada. Plus, free two-day shipping for six months when you sign up for Amazon Prime for : an Boudrez. Buy Interaction of the Protein Phosphatase-1 Regulator NIPP1 with Pre-mRNA Splicing Factors (Acta Biomedica Lovaniensia) 01 by An Boudrez (ISBN: ) from Amazon's Book Store. Everyday low prices and free delivery on eligible : An Boudrez.   Protein phosphatase 1 (PP1) and protein phosphatase 2Cgamma associate with complexes formed on pre-mRNA and can be identified in the B complex. PP1 or PP2A-mediated dephosphorylation are involved in the structural rearrangements that are necessary for the transition from the first to second step of splicing. However, the binding partners and Cited by: Protein phosphatase 1 is abundantly expressed in the nucleus, where it is complexed with a variety of regulatory subunits to control such processes as cell-cycle progression and division, transcription, and pre-mRNA splicing. Sds22, a protein required for exit from mitosis, and HCF-1 (human factor C1) have no discernable RVXF motif. Disruption Cited by: 5.

  Phosphorylation of splicing factors modulates their interaction with binding partners during splicing and also appears to facilitate the spliceosome dynamics at every step of the splicing reaction []. All phosphorylation in the spliceosome detected to date takes place on serine and/or threonine by: 9. This protein has been demonstrated to act as a positive regulator of cell cycle G 2 /M progression. It was also found to be an essential component of a non-snRNA spliceosome, which contains at least five additional protein factors and is required for the second catalytic step of pre-mRNA splicing. InteractionsAliases: CDC5L, CDC5, CDC5-LIKE, CEF1, . C6 pyridinium ceramide influences alternative pre-mRNA splicing by inhibiting protein phosphatase-1 Article (PDF Available) in Nucleic Acids Research 40(9) . The nuclear inhibitor of protein phosphatase 1 -NIPP1 is included in the family of protein phosphatase 1 -PP1, regulatory proteins [73,74] and was shown to .