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

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Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity.

We have purified a form of protein phosphatase 1 ( PP1) from HeLa cell nuclei, in which the phosphatase is complexed to a regulatory subunit termed p99. We report here the cloning and characterisation of the p99 component. p99 mRNA is widely expressed in human tissues and immunofluorescence analysis with anti-p99 antibodies showed a punctate nucleoplasmic staining with additional accumulations within the nucleolus. The C-terminus of p99 contains seven RGG RNA-binding motifs, followed by eleven decapeptide repeats containing six or more of the following conserved residues (GHRPHEGPGG), and finally a putative zinc finger domain. Recombinant p99 suppresses the phosphorylase phosphatase activity of PP1 by > 90% and the canonical PP1- binding motif on p99 (residues 396-401) is unusual in that the phenylalanine residue is replaced by tryptophan.[1]

References

  1. Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity. Kreivi, J.P., Trinkle-Mulcahy, L., Lyon, C.E., Morrice, N.A., Cohen, P., Lamond, A.I. FEBS Lett. (1997) [Pubmed]
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