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Erschienen in: Journal of Neural Transmission 12/2014

01.12.2014 | Translational Neurosciences - Review article

Complex molecular regulation of tyrosine hydroxylase

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

Erschienen in: Journal of Neural Transmission | Ausgabe 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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Metadaten
Titel
Complex molecular regulation of tyrosine hydroxylase
verfasst von
Izel Tekin
Robert Roskoski Jr.
Nurgul Carkaci-Salli
Kent E. Vrana
Publikationsdatum
01.12.2014
Verlag
Springer Vienna
Erschienen in
Journal of Neural Transmission / Ausgabe 12/2014
Print ISSN: 0300-9564
Elektronische ISSN: 1435-1463
DOI
https://doi.org/10.1007/s00702-014-1238-7

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