Protein kinase C phosphorylation of threonine at position 888 in Ca2+o-sensing receptor (CaR) inhibits coupling to Ca2+ store release.

@article{Bai1998ProteinKC,
  title={Protein kinase C phosphorylation of threonine at position 888 in Ca2+o-sensing receptor (CaR) inhibits coupling to Ca2+ store release.},
  author={Mengting Bai and Seema Trivedi and Coldharbour Lane and Yong-ping Yang and S. J. Quinn and Edward Meigs Brown},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 33},
  pages={
          21267-75
        }
}
Previous studies in parathyroid cells, which express the G protein-coupled, extracellular calcium-sensing receptor (CaR), showed that activation of protein kinase C (PKC) blunts high extracellular calcium (Ca2+o)-evoked stimulation of phospholipase C and the associated increases in cytosolic calcium (Ca2+i), suggesting that PKC may directly modulate the coupling of the CaR to intracellular signaling systems. In this study, we examined the role of PKC in regulating the coupling of the CaR to Ca2… CONTINUE READING
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