Tyrosine hydroxylase phosphorylation: regulation and consequences

@article{Dunkley2004TyrosineHP,
  title={Tyrosine hydroxylase phosphorylation: regulation and consequences},
  author={Peter R Dunkley and Larisa Bobrovskaya and Mark Evan Graham and Ellak I. von Nagy-Felsobuki and Phillip W Dickson},
  journal={Journal of Neurochemistry},
  year={2004},
  volume={91}
}
The rate‐limiting enzyme in catecholamine synthesis is tyrosine hydroxylase. It is phosphorylated at serine (Ser) residues Ser8, Ser19, Ser31 and Ser40 in vitro, in situ and in vivo. A range of protein kinases and protein phosphatases are able to phosphorylate or dephosphorylate these sites in vitro. Some of these enzymes are able to regulate tyrosine hydroxylase phosphorylation in situ and in vivo but the identity of the kinases and phosphatases is incomplete, especially for physiologically… 
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TLDR
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TLDR
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TLDR
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TLDR
The myriad mechanisms that regulate tyrosine hydroxylase expression and activity are revisited and their physiological importance in the control of catecholamine biosynthesis is highlighted.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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