Crossref journal-article
Wiley
FEBS Letters (311)
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.

Bibliography

Kreivi, J.-P., Trinkle-Mulcahy, L., Lyon, C. E., Morrice, N. A., Cohen, P., & Lamond, A. I. (1997). Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity. FEBS Letters, 420(1), 57–62. Portico.

Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 11:03 a.m.)
Deposited 1 year, 11 months ago (Sept. 16, 2023, 8:36 a.m.)
Indexed 3 weeks, 3 days ago (Aug. 5, 2025, 8:58 a.m.)
Issued 27 years, 8 months ago (Dec. 22, 1997)
Published 27 years, 8 months ago (Dec. 22, 1997)
Published Online 27 years, 7 months ago (Jan. 20, 1998)
Published Print 27 years, 8 months ago (Dec. 22, 1997)
Funders 0

None

@article{Kreivi_1997, title={Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity}, volume={420}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(97)01485-3}, DOI={10.1016/s0014-5793(97)01485-3}, number={1}, journal={FEBS Letters}, publisher={Wiley}, author={Kreivi, Jan-Peter and Trinkle-Mulcahy, Laura and Lyon, Carol E and Morrice, Nick A and Cohen, Philip and Lamond, Angus I}, year={1997}, month=dec, pages={57–62} }