Tyrosine hydroxylase phosphorylation in  vivo

Tyrosine hydroxylase (TH) is the rate ‐limiting enzyme in catecholamine synthesis. Its activity is controlled by protein phosphorylation. This review summarises: The methods used to investigate TH phosphorylation and TH activationin  vivo. Thein  vivo evidence for: Which protein kinases phosphorylate TH? Which protein phosphatases dephosphorylate TH? What is the stoichiometry of pTH? What proteins bind to pTH? Where is pTH localised? What is the nature of TH regulation in different catecholaminergic cells? The time course of TH phosphorylationin  vivo in response to stressors activating major catecholaminergic cell groups. AbstractTyrosine hydroxylase (TH) is the rate ‐limiting enzyme in the synthesis of the catecholamines dopamine, noradrenaline and adrenaline. One of the major mechanisms for controlling the activity of TH is protein phosphorylation. TH is phosphorylated at serine residues 8, 19, 31 and 40. There have been a number of previous reviews focused on TH phosphorylationin  vitro andin  situ. This review on TH phosphorylationin  vivo has three main sections focusing on: (1) the methods used to investigate TH phosphorylationin  vivo, including the animals used, the sacrifice procedures, the tissue preparation, the measurement of TH protein levels and TH phosphorylation and the measurement of TH activation. (2) The regulation of TH phosphorylation and its consequencesin  vivo, including the kinases and phosphatases acting on TH, the stoichiome...
Source: Journal of Neurochemistry - Category: Neuroscience Authors: Tags: Review Source Type: research