- Title
- Tyrosine hydroxylase phosphorylation in vivo
- Creator
- Dunkley, Peter R.; Dickson, Phillip W.
- Relation
- Journal of Neurochemistry Vol. 149, Issue 6, p. 706-728
- Publisher Link
- http://dx.doi.org/10.1111/jnc.14675
- Publisher
- Wiley
- Resource Type
- journal article
- Date
- 2019
- Description
- Tyrosine 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 phosphorylation in vitro and in situ. This review on TH phosphorylation in vivo has three main sections focusing on: (1) the methods used to investigate TH phosphorylation in 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 consequences in vivo, including the kinases and phosphatases acting on TH, the stoichiometry of TH phosphorylation, the proteins that bind TH and TH subcellular location. (3) The acute and prolonged TH phosphorylation changes in specific catecholaminergic tissues, including the adrenal medulla, the nigrostriatal pathway and the mesolimbic pathway.
- Subject
- catecholamines; consequences; in vivo; phosphorylation; regulation; tyrosine hydroxylase
- Identifier
- http://hdl.handle.net/1959.13/1410583
- Identifier
- uon:36204
- Identifier
- ISSN:0022-3042
- Rights
- This is the peer reviewed version of the above article, which has been published in final form at: http://dx.doi.org/10.1111/jnc.14675. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
- Language
- eng
- Full Text
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