Phorbol-ester-activated protein kinase C-alpha lacking phosphorylation at Ser657 is down-regulated by a mechanism involving dephosphorylation.

@article{Gysin1997PhorbolesteractivatedPK,
  title={Phorbol-ester-activated protein kinase C-alpha lacking phosphorylation at Ser657 is down-regulated by a mechanism involving dephosphorylation.},
  author={S Gysin and Roland Imber},
  journal={European journal of biochemistry},
  year={1997},
  volume={249 1},
  pages={156-60}
}
Protein kinase C (PKC) is a key enzyme in the intracellular signaling network. Upon activation by 12-O-tetradecanoylphorbol 13-acetate, the alpha-isoform of PKC translocates to the detergent-soluble and the detergent-insoluble fractions. Besides cofactors, the activity and stability of this protein is critically regulated by multisite phosphorylations. At least three distinct sites, Thr497, Thr638 and Ser657, are involved. We have previously shown that the replacement of Ser657 by alanine leads… CONTINUE READING

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