Ontology highlight
ABSTRACT:
SUBMITTER: Chamousset D
PROVIDER: S-EPMC2993749 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Chamousset Delphine D De Wever Veerle V Moorhead Greg B GB Chen Yan Y Boisvert Francois-Michel FM Lamond Angus I AI Trinkle-Mulcahy Laura L
Molecular biology of the cell 20101006 23
A pool of protein phosphatase 1 (PP1) accumulates within nucleoli and accounts for a large fraction of the serine/threonine protein phosphatase activity in this subnuclear structure. Using a combination of fluorescence imaging with quantitative proteomics, we mapped the subnuclear localization of the three mammalian PP1 isoforms stably expressed as GFP-fusions in live cells and identified RRP1B as a novel nucleolar targeting subunit that shows a specificity for PP1β and PP1γ. RRP1B, one of two m ...[more]