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- W2124275588 abstract "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." @default.
- W2124275588 created "2016-06-24" @default.
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- W2124275588 date "1997-12-22" @default.
- W2124275588 modified "2023-10-16" @default.
- W2124275588 title "Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity" @default.
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- W2124275588 doi "https://doi.org/10.1016/s0014-5793(97)01485-3" @default.
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