Sustained phosphorylation of tyrosine hydroxylase at serine 40: a novel mechanism for maintenance of catecholamine synthesis

@article{Bobrovskaya2007SustainedPO,
  title={Sustained phosphorylation of tyrosine hydroxylase at serine 40: a novel mechanism for maintenance of catecholamine synthesis},
  author={Larisa Bobrovskaya and Conor Gilligan and Ellen K Bolster and Jeffrey J Flaherty and Phillip W Dickson and Peter R Dunkley},
  journal={Journal of Neurochemistry},
  year={2007},
  volume={100}
}
Tyrosine hydroxylase (TH) is the rate‐limiting enzyme in catecholamine synthesis. Its activity is known to be controlled acutely (minutes) by phosphorylation and chronically (days) by protein synthesis. Using bovine adrenal chromaffin cells we found that nicotine, acting via nicotinic receptors, sustained the phosphorylation of TH at Ser40 for up to 48 h. Nicotine also induced sustained activation of TH, which for the first 24 h was completely independent of TH protein synthesis, and the… 
Tyrosine hydroxylase phosphorylation in vivo
TLDR
This review on TH phosphorylation in vivo has three main sections focusing on: the methods used to investigate TH phosphate levels in vivo, the animals used, the sacrifice procedures, the tissue preparation, the measurement of TH protein levels and THosphorylation and the measurements of TH activation.
The Sustained Phase of Tyrosine Hydroxylase Activation In vivo
TLDR
Evidence is provided for the first time that TH phosphorylation at Ser31 and Ser40 occurs for up to 24 h in vivo and leads to TH activation independent of TH protein synthesis, suggesting that the sustained phase of TH activation occurs in vivo.
Retinol activates tyrosine hydroxylase acutely by increasing the phosphorylation of serine40 and then serine31 in bovine adrenal chromaffin cells
TLDR
The results show that retinol activates tyrosine hydroxylase via two sequential non‐genomic mechanisms, which have not previously been characterized, likely to operate in vivo to facilitate the stress response, especially when vitamin supplements are taken or when Retinol is used as a therapeutic agent.
Manganese induces sustained Ser40 phosphorylation and activation of tyrosine hydroxylase in PC12 cells
TLDR
Sustained TH phosphorylation at Ser40 and the consequent activation of TH both occurred at low concentrations of Mn2- and this provides a potential new mechanism for Mn2+‐induced neuronal action that does not involve H2O2‐mediated cell death.
Tyrosine hydroxylase activity is regulated by two distinct dopamine‐binding sites
Tyrosine hydroxylase (TH), the rate‐limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines
Phosphorylation and activation of tryptophan hydroxylase 2: identification of serine‐19 as the substrate site for calcium, calmodulin‐dependent protein kinase II
TLDR
Results establish that activation of TPH2 by CaMKII is mediated by phosphorylation of serine‐19 within the regulatory domain of the enzyme.
The Effect of Social Defeat on Tyrosine Hydroxylase Phosphorylation in the Rat Brain and Adrenal Gland
TLDR
The findings suggest that the regulation of TH phosphorylation in different catecholamine-producing cells varies considerably and is dependent on both the nature of the stressor and the time at which the response is analysed.
Pattern-specific sustained activation of tyrosine hydroxylase by intermittent hypoxia: role of reactive oxygen species-dependent downregulation of protein phosphatase 2A and upregulation of protein kinases.
TLDR
It is demonstrated that IH in a pattern-specific manner activates TH involving ROS-mediated sustained increase in TH phosphorylation via downregulation of PP2A and upregulation of protein kinases.
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References

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TLDR
H hierarchical phosphorylation provides a mechanism whereby the two major human TH isoforms can be differentially regulated with only isoform 1 responding to the ERK pathway, whereas isoform 2 is more sensitive to calcium-mediated events.
Tyrosine hydroxylase phosphorylation: regulation and consequences
TLDR
Hierarchical phosphorylation of tyrosine hydroxylase occurs both in vitro and in situ, whereby theosphorylation at Ser19 increases the rate of Ser40 phosphorylated leading to an increase in enzyme activity.
Neurotensin induces tyrosine hydroxylase gene activation through nitric oxide and protein kinase C signaling pathways.
TLDR
It is demonstrated, by quantitative reverse transcription-polymerase chain reaction, gel shift, and protein assays, that TH gene activation by NT agonist requires both protein kinase C stimulation and nitric oxide production.
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TLDR
The data indicate that the mobilization of intracellular Ca2+ plays a crucial role in supporting H1‐mediated TOH phosphorylation and may thus have a potentially important role in regulating catecholamine synthesis.
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TLDR
Regulatory mechanisms provide not only redundancy but also diversity in the control of catecholamine biosynthesis.
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TLDR
Evidence is provided for a mutual interaction between the presumed regulatory and catalytic domains of hTH, and it is shown that activation of the enzyme by phosphorylation and inactivation by binding of catecholamines are related events, which probably represent important mechanisms for the regulation of the enzymes activity in vivo.
Multiple signaling pathways in bovine chromaffin cells regulate tyrosine hydroxylase phosphorylation at Ser19, Ser31, and Ser40
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  • Biology, Chemistry
    Neurochemical Research
  • 2004
TLDR
The phosphorylation of TH in bovine chromaffin cells appears to be regulated at three sites by three separate intracellular signaling pathways—Ser19 via Ca2+/calmodulin-dependent protein kinase II; Ser31 via ERK (MAP2 kinases); and Ser40 via cAMP-dependentprotein kinase.
Histamine activates tyrosine hydroxylase in bovine adrenal chromaffin cells through a pathway that involves ERK1/2 but not p38 or JNK
TLDR
The hypothesis that the up‐regulation of the ERK1/2 pathway, but not that of p38 or JNK, promoted by histamine is involved in the phosphorylation of TH at Ser31 is supported and that this phosphorylated event is required for the full activation of this enzyme.
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