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Published in: Journal of Neural Transmission 12/2014

01-12-2014 | Translational Neurosciences - Review article

Complex molecular regulation of tyrosine hydroxylase

Authors: Izel Tekin, Robert Roskoski Jr., Nurgul Carkaci-Salli, Kent E. Vrana

Published in: Journal of Neural Transmission | Issue 12/2014

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Abstract

Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, is strictly controlled by several interrelated regulatory mechanisms. Enzyme synthesis is controlled by epigenetic factors, transcription factors, and mRNA levels. Enzyme activity is regulated by end-product feedback inhibition. Phosphorylation of the enzyme is catalyzed by several protein kinases and dephosphorylation is mediated by two protein phosphatases that establish a sensitive process for regulating enzyme activity on a minute-to-minute basis. Interactions between tyrosine hydroxylase and other proteins introduce additional layers to the already tightly controlled production of catecholamines. Tyrosine hydroxylase degradation by the ubiquitin–proteasome coupled pathway represents yet another mechanism of regulation. Here, we revisit the myriad mechanisms that regulate tyrosine hydroxylase expression and activity and highlight their physiological importance in the control of catecholamine biosynthesis.
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Metadata
Title
Complex molecular regulation of tyrosine hydroxylase
Authors
Izel Tekin
Robert Roskoski Jr.
Nurgul Carkaci-Salli
Kent E. Vrana
Publication date
01-12-2014
Publisher
Springer Vienna
Published in
Journal of Neural Transmission / Issue 12/2014
Print ISSN: 0300-9564
Electronic ISSN: 1435-1463
DOI
https://doi.org/10.1007/s00702-014-1238-7

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