Enhancement of tyrosine hydroxylase phosphorylation and activity by glial cell line-derived neurotrophic factor.

@article{Kobori2004EnhancementOT,
  title={Enhancement of tyrosine hydroxylase phosphorylation and activity by glial cell line-derived neurotrophic factor.},
  author={Nobuhide Kobori and Jack C. Waymire and John W Haycock and Guy L. Clifton and Pramod K Dash},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 3},
  pages={2182-91}
}
Although glial cell-line derived neurotrophic factor (GDNF) acts as a potent survival factor for dopaminergic neurons, it is not known whether GDNF can directly alter dopamine synthesis. Tyrosine hydroxylase (TH) is the rate-limiting enzyme for dopamine biosynthesis, and its activity is regulated by phosphorylation on three seryl residues: Ser-19, Ser-31, and Ser-40. Using a TH-expressing human neuroblastoma cell line and rat primary mesencephalic neuron cultures, the present study examined… CONTINUE READING
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GDNF Increases TH Phosphorylation and Enzymatic Activity 2191 by gest on A ril 30, 2016 hp://w w w .jb.org/ D

  • J. W. Haycock, N. G. Ahn, M. H. Cobb, E. G. Krebs
  • J. Biol. Chem. 10.1074/jbc.M310734200
  • 1992
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