
The sensitivity of PKC alpha to two protein phosphatases (PP1 and PP2A) has been studied. The results show that both phosphatases reversibly inhibit PKC alpha activity suggesting an effect at PKC autophosphorylation sites and not at transphosphorylation sites. Moreover, PP1 has been found at low concentration to activate PKC alpha implying the existence of an inhibitory phosphorylation site. Further, PKC alpha has been shown to phosphorylate PP2A at its regulatory subunit B.
Protein Kinase C-alpha, Membrane Proteins, Recombinant Proteins, Enzyme Activation, Isoenzymes, Adenosine Triphosphate, Protein Phosphatase 1, Phosphoprotein Phosphatases, Protein Phosphatase 2, Phosphorylation, Protein Kinase C
Protein Kinase C-alpha, Membrane Proteins, Recombinant Proteins, Enzyme Activation, Isoenzymes, Adenosine Triphosphate, Protein Phosphatase 1, Phosphoprotein Phosphatases, Protein Phosphatase 2, Phosphorylation, Protein Kinase C
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