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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Background
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BackgroundInfluential
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“Ser(40)dephosphorylation by protein phosphatase 2A (PP2A) results in decreased TH activity [33].”
Background
Fluorescence Spectroscopy as a Probe of the Effect of Phosphorylation at Serine 40 of Tyrosine Hydroxylase on the Conformation of Its Regulatory Domain
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Early Life Stress and Post-Weaning High Fat Diet Alter Tyrosine Hydroxylase Regulation and AT1 Receptor Expression in the Adrenal Gland in a Sex Dependent Manner
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“In the longer term TH is regulated by increases in TH protein which allow greater activation of TH [42].”
BackgroundInfluentialSelf-citation
Short-term Effects of Endothelins on Tyrosine Hydroxylase Activity and Expression in the Olfactory Bulb of Normotensive Rats
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“Tyrosine hydroxylase (TH) is the enzyme that catalyzes the rate-limiting step in the synthesis of catecholamines and its activity is tightly controlled by diverse mechanisms [19–21].”
BackgroundInfluential
Development of an enzyme-linked immunosorbent assay (ELISA) to measure the level of tyrosine hydroxylase protein in brain tissue from Parkinson's disease models
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“We also examined the state of TH phosphorylation on Ser31 and Ser40, sites that are thought to affect TH activity (Dunkley et al. 2004; Daubner et al. 2011) and TH turnover (Nakashima et al. 2011).”
BackgroundInfluential
Dopac distribution and regulation in striatal dopaminergic varicosities and extracellular space
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“For example, activation of pre-synaptic dopamine D2 receptors is thought to lessen the extent of phosphorylation of Ser40 on the tyrosine hydroxylase protein, resulting in a decreased rate of dopamine synthesis (Dunkley et al., 2004; Lindgren et al., 2001, 2002).”
Background
Transforming growth factor-beta in the brain enhances fat oxidation via noradrenergic neurons in the ventromedial and paraventricular hypothalamic nucleus
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Stabilization of Human Tyrosine Hydroxylase in Maltodextrin Nanoparticles for Delivery to Neuronal Cells and Tissue
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Role of the HIF‐1α/Nur77 axis in the regulation of the tyrosine hydroxylase expression by insulin in PC12 cells
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“Phosphorylated tyrosine hydroxylase (pTH) at Ser40 is positively related to the speed of dopamine synthesis (Dunkley et al., 2004) and HI animals had higher expression of pTH in both PFC hemispheres, indicating an increase in DA synthesis.”
L-Tyr-Induced Phosphorylation of Tyrosine Hydroxylase at Ser40: An Alternative Route for Dopamine Synthesis and Modulation of Na+/K+-ATPase in Kidney Cells
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“Iron is not only an essential micronutrient required for oxygen transport, it is also a required cofactor for key enzymes in neurotransmitter production (Beard, 2003; Dunkley et al., 2004; Wang et al., 2002).”
Oral l ‐tyrosine supplementation augments the vasoconstriction response to whole‐body cooling in older adults
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“In an ‘activated state’, such as during cold or exercise stress, TH ultimately depends on increased bioavailability of both the amino acid substrate and the pterin cofactor (Kumer & Vrana, 1996; Dunkley et al. 2004).”
Background
Endogenous tetrahydroisoquinolines associated with Parkinson’s disease mimic the feedback inhibition of tyrosine hydroxylase by catecholamines
Scholz, J., Toska, K., Luborzewski, A., Maaß, A., Schünemann, V., Haavik, J., & Moser, A. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06365.x · Cited by 12
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Effects of ERK1/2 kinases inactivation on the nigrostriatal system of Krushinsky-Molodkina rats genetically prone to audiogenic seizures
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Acute salt loading induces sympathetic nervous system overdrive in mice lacking salt-inducible kinase 1 (SIK1)
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The Effects of Chronic Unpredictable Mild Stress and Semi-Pure Diets on the Brain, Gut and Adrenal Medulla in C57BL6 Mice
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“According to Dunkley et al. [86], Ser31 phosphatases require the inactivation of kinases (such as ERK1/2).”
BackgroundSelf-citation
Immobilization of Aspergillus oryzae tyrosine hydroxylase on ZnO nanocrystals for improved stability and catalytic efficiency towards L-dopa production
Khalid, A., Ali, S., Rukhma, et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-50198-x · Cited by 11
Chronic Blockade of Brain Endothelin Receptor Type-A (ETA) Reduces Blood Pressure and Prevents Catecholaminergic Overactivity in the Right Olfactory Bulb of DOCA-Salt Hypertensive Rats
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“The specific marker of catecholaminergic neurons is TH, which catalyzes the rate limiting step in catecholamine biosynthesis [35,36].”
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N‐Propanoylmannosamine interferes with O‐GlcNAc modification of the tyrosine 3‐monooxygenase and stimulates dopamine secretion
Bork, K., Kannicht, C., Nöhring, S., Reutter, W. G., Weidemann, W., Hart, G. W., & Horstkorte, R. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21526 · Cited by 11
“The enzymatic activity of tyrosine 3-monooxygenase is up-regulated by phosphorylation (Dunkley et al., 2004).”
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Enhanced tyrosine hydroxylase phosphorylation in the nucleus accumbens and nucleus tractus solitarius-A2 cell group after morphine-conditioned place preference
Cuello, A. M. G., Mora, L., Hidalgo, J. M., Meca, N., Lasheras, C., Milanés, M. V., & Laorden, M. L. (2010) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-010-0567-9 · Cited by 11
“Short-term regulation of catecholamines biosynthesis occurs through phosphorylation of TH, which enhances enzymatic activity (Dunkley et al. 2004).”
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Effects of Electroacupuncture on Methamphetamine‐Induced Behavioral Changes in Mice
Ho, T., Lee, C., Lu, Z., Lane, H., Tsai, M.-H., Ho, I.-K., Huang, C., & Chiang, Y. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/5642708 · Cited by 11
“A study suggested that TH phosphorylation can increase its enzyme activity [20].”
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Regulation of tyrosine hydroxylase: relevance to Parkinson's disease
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“Additionally, DA release is tightly coupled to synthesis, whereby end-product feedback inhibition decreases the rate of DA synthesis, and phosphorylation of tyrosine hydroxylase (TH) increases it (Dunkley et al., 2004).”
Background
EPHB6 controls catecholamine biosynthesis by up-regulating tyrosine hydroxylase transcription in adrenal gland chromaffin cells
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Niacin, an innovative protein kinase-C-dependent endoplasmic reticulum stress reticence in murine Parkinson's disease
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The Low Affinity Dopamine Binding Site on Tyrosine Hydroxylase: The Role of the N-Terminus and In Situ Regulation of Enzyme Activity
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NT5DC2 affects the phosphorylation of tyrosine hydroxylase regulating its catalytic activity
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Interferon‐α Signalling in Bovine Adrenal Chromaffin Cells: Involvement of Signal‐Transducer and Activator of Transcription 1 and 2, Extracellular Signal‐Regulated Protein Kinases 1/2 and Serine 31 Phosphorylation of Tyrosine Hydroxylase
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Iron Deficiency and Neuropharmacology
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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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