Protein kinase C-beta activates tyrosinase by phosphorylating serine residues in its cytoplasmic domain.

@article{Park1999ProteinKC,
  title={Protein kinase C-beta activates tyrosinase by phosphorylating serine residues in its cytoplasmic domain.},
  author={Hee-Young Park and Jose Manuel Perez and Richard A. Laursen and Masaki Hara and Barbara A. Gilchrest},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 23},
  pages={16470-8}
}
We have previously shown that protein kinase C-beta (PKC-beta) is required for activation of tyrosinase (Park, H. Y., Russakovsky, V., Ohno, S., and Gilchrest, B. A. (1993) J. Biol. Chem. 268, 11742-11749), the rate-limiting enzyme in melanogenesis. We now examine its mechanism of activation in human melanocytes. In vivo phosphorylation experiments revealed that tyrosinase is phosphorylated through the PKC-dependent pathway and that introduction of PKC-beta into nonpigmented human melanoma… CONTINUE READING