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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

PPP1R8  -  protein phosphatase 1, regulatory subunit 8

Bos taurus

 
 
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High impact information on PPP1R8

  • The catalytic subunit of protein phosphatase-1 did not bind to poly(U)-Sepharose, but it bound very tightly after complexation with NIPP-1 [1].
  • These data are in agreement with a function of NIPP-1 in targeting protein phosphatase-1 to RNA [1].
  • Phosphorylation decreased the binding of NIPP-1 to immobilized protein phosphatase-1 [2].
  • Bovine thymus nuclei contain a species of protein phosphatase-1 (PP-1N alpha) that can be partially activated by phosphorylation of an associated inhibitory polypeptide, NIPP-1, with protein kinase A [Beullens, Van Eynde, Bollen and Stalmans (1993) J. Biol. Chem. 268, 13172-13177] [3].
  • Casein kinase-2 introduced up to 1.2 phosphate groups into purified NIPP-1 on serine and threonine residues [3].
 

Analytical, diagnostic and therapeutic context of PPP1R8

  • We report here that baculovirus-expressed recombinant NIPP-1 displays RNA-binding properties, as revealed by North-Western analysis, by UV-mediated cross-linking, by RNA mobility-shift assays, and by chromatography on poly(U)-Sepharose [1].

References

  1. NIPP-1, a nuclear inhibitory subunit of protein phosphatase-1, has RNA-binding properties. Jagiello, I., Beullens, M., Vulsteke, V., Wera, S., Sohlberg, B., Stalmans, W., von Gabain, A., Bollen, M. J. Biol. Chem. (1997) [Pubmed]
  2. Inactivation of nuclear inhibitory polypeptides of protein phosphatase-1 (NIPP-1) by protein kinase A. Beullens, M., Van Eynde, A., Bollen, M., Stalmans, W. J. Biol. Chem. (1993) [Pubmed]
  3. Full activation of a nuclear species of protein phosphatase-1 by phosphorylation with protein kinase A and casein kinase-2. Van Eynde, A., Beullens, M., Stalmans, W., Bollen, M. Biochem. J. (1994) [Pubmed]
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