Cited by 456Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingNeurotransmitter Receptor Influence on Behavior

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Tyrosine hydroxylase phosphorylation: regulation and consequences

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Dunkley, Peter R., Bobrovskaya, Larisa, Graham, Mark E., Von Nagy‐Felsobuki, Ellak I., Dickson, Phillip W.·2004·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2004.02797.x

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Abstract

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 relevant stimuli. The stoichiometry of tyrosine hydroxylase phosphorylation in situ and in vivo is low. The phosphorylation of tyrosine hydroxylase at Ser40 increases the enzyme's activity in vitro, in situ and in vivo. Phosphorylation at Ser31 also increases the activity but to a much lesser extent than for Ser40 phosphorylation. The phosphorylation of tyrosine hydroxylase at Ser19 or Ser8 has no direct effect on tyrosine hydroxylase activity. Hierarchical phosphorylation of tyrosine hydroxylase occurs both in vitro and in situ, whereby the phosphorylation at Ser19 increases the rate of Ser40 phosphorylation leading to an increase in enzyme activity. Hierarchical phosphorylation depends on the state of the substrate providing a novel form of control of tyrosine hydroxylase activation.

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“It should also be noted that Ca 2+ dependent phosphorylation of TH (Dunkley et al., 2004) is likely to play a role in the absence of exogenously added L-DOPA.”

See all 456

Authors: Dunkley, P. R., Bobrovskaya, L., Graham, M. E., Von Nagy‐Felsobuki, E. I., & Dickson, P. W.
Affiliations: University of Newcastle Australia (AU)
Corresponding author: Dunkley, Peter R.
ORCID: Dunkley, Peter R.
Bobrovskaya, Larisa
Graham, Mark E.
Dickson, Phillip W.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2004-11-18
Volume: 91
Issue: 5
Pages: 1025-1043
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2004.02797.x
OpenAlex: W2114431124
Semantic Scholar: f10f568903c3e4d7cdc660f6816f0563cabf919f
Cited by: 455
References: 117
Citations by year: 2026: 6 · 2025: 12 · 2024: 13 · 2023: 16 · 2022: 8 · 2021: 23 · 2020: 19 · 2019: 26 · 2018: 20 · 2017: 23 · 2016: 19 · 2015: 29 · 2014: 24 · 2013: 32 · 2012: 28
FWCI: 1.16
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: Medical Research Council
National Health and Medical Research Council
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurotransmitter Receptor Influence on Behavior
Keywords: tyrosine hydroxylase, serine phosphorylation, catecholamine synthesis, protein kinases, protein phosphatase, enzyme activation, phosphorylation stoichiometry
MeSH terms: Animals, Models, Biological, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Serine, Tyrosine 3-Monooxygenase

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Tyrosine hydroxylase phosphorylation: regulation and consequences

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