Phosphorylation of protein kinase C sites in NBD1 and the R domain control CFTR channel activation by PKA.

@article{Chappe2003PhosphorylationOP,
  title={Phosphorylation of protein kinase C sites in NBD1 and the R domain control CFTR channel activation by PKA.},
  author={Val{\'e}rie Chappe and Deborah A R Hinkson and Tang Zhu and X-B Chang and John R. Riordan and John W. Hanrahan},
  journal={The Journal of physiology},
  year={2003},
  volume={548 Pt 1},
  pages={39-52}
}
Activation of the cystic fibrosis transmembrane conductance regulator (CFTR) channel by protein kinase A (PKA) is enhanced by protein kinase C (PKC). However, the mechanism of modulation is not known and it remains uncertain whether PKC acts directly on CFTR or through phosphorylation of an ancillary protein. Using excised patches that had been pre-treated with phosphatases, we found that PKC exposure results in much larger PKA-activated currents and shifts the PKA concentration dependence. To… CONTINUE READING

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