PACAP stimulates the sustained phosphorylation of tyrosine hydroxylase at serine 40.

@article{Bobrovskaya2007PACAPST,
  title={PACAP stimulates the sustained phosphorylation of tyrosine hydroxylase at serine 40.},
  author={Larisa Bobrovskaya and Daniel Pens Gelain and Conor Gilligan and Phillip W. Dickson and Peter Dunkley},
  journal={Cellular signalling},
  year={2007},
  volume={19 6},
  pages={1141-9}
}
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine synthesis. Its activity is controlled by PACAP, acutely by phosphorylation at Ser40 and chronically by protein synthesis. Using bovine adrenal chromaffin cells we found that PACAP, acting via the continuous activation of PACAP 1 receptors, sustained the phosphorylation of TH at Ser40 and led to TH activation for up to 24 h in the absence of TH protein synthesis. The sustained phosphorylation of TH at Ser40 was not mediated… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

Similar Papers

Loading similar papers…