Protein kinase C (PKC) phosphorylation of the Ca2+ o-sensing receptor (CaR) modulates functional interaction of G proteins with the CaR cytoplasmic tail.

@article{Jiang2002ProteinKC,
  title={Protein kinase C (PKC) phosphorylation of the Ca2+ o-sensing receptor (CaR) modulates functional interaction of G proteins with the CaR cytoplasmic tail.},
  author={Yong-Feng Jiang and Zaixiang Zhang and Olga Kifor and C. Rickword Lane and S. J. Quinn and M. Geetha Bai},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 52},
  pages={50543-9}
}
The extracellular calcium (Ca(2+)(o))-sensing receptor (CaR) activates Ca(2+) influx independent of the release of intracellular Ca(2+) stores. The latter can be negatively regulated by protein kinase C (PKC) through phosphorylation of Thr-888 of the CaR. In this study, we substituted Thr-888 with various amino acid residues or a stop codon to understand how PKC phosphorylation of the CaR inhibits receptor-mediated release of intracellular Ca(2+) stores. Substitutions of Thr-888 with… CONTINUE READING

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