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The protein phosphatases PP1 c , PP2A c and PP2Cα are shown to dephosphorylate protein kinase Cδ (PKCδ) in vitro; of these PP2A c displayed the highest specific activity towards PKCδ. The role of PP2A c in the dephosphorylation of PKCδ in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells. However the observation...
Cdc25C phosphatase induces mitosis by dephosphorylating and activating Cdc2/cyclin B protein kinase. Phosphorylation of Xenopus Cdc25C at serine 287 creates a binding site for a 14-3-3 protein and restrains activation during interphase. Here, we show that dephosphorylation of S287 is catalysed by protein phosphatase-2A in Xenopus egg extracts. 14-3-3 protein binding to Cdc25C inhibits dephosphorylation...
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