Abstract
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 that binding of Mg-ATP to PKCδ could protect the enzyme from dephosphorylation by PP2A c in vitro indicates that an additional input/factor is required for dephosphorylation in vivo.
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