ArticleNeurochemical research2002
Tyrosine hydroxylase dephosphorylation by protein phosphatase 2A in bovine adrenal chromaffin cells.
Article in Neurochemical research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Pathogenic Impact of Fatty Acid-Binding Proteins in Parkinson's Disease-Potential Biomarkers and Therapeutic Targets.International journal of molecular sciences · 2023Review
- "Janus-Faced" α-Synuclein: Role in Parkinson's Disease.Frontiers in cell and developmental biology · 2021Review
- Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson's Disease and Dopa-Responsive Dystonia.International journal of molecular sciences · 2020Review
- Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins.Amino acids · 2016Article
- Protein phosphatase 2A is involved in the tyrosine hydroxylase phosphorylation regulated by α-synuclein.Neurochemical research · 2015Article
- Complex molecular regulation of tyrosine hydroxylase.Journal of neural transmission (Vienna, Austria : 1996) · 2014Review
- Complexity of dopamine metabolism.Cell communication and signaling : CCS · 2013Article
- Lewy-like aggregation of α-synuclein reduces protein phosphatase 2A activity in vitro and in vivo.Neuroscience · 2012Article
- Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A.PloS one · 2011Article
- Serine 129 phosphorylation reduces the ability of alpha-synuclein to regulate tyrosine hydroxylase and protein phosphatase 2A in vitro and in vivo.The Journal of biological chemistry · 2010Article
- Progesterone decreases tyrosine hydroxylase phosphorylation state and increases protein phosphatase 2A activity in the stalk-median eminence on proestrous afternoon.The Journal of endocrinology · 2010Article
- Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin-proteasome system in PC12D cells.Journal of neural transmission (Vienna, Austria : 1996) · 2009Article
- 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.Antioxidants & redox signaling · 2009Article
- Protein kinase C delta negatively regulates tyrosine hydroxylase activity and dopamine synthesis by enhancing protein phosphatase-2A activity in dopaminergic neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Dynamics of tyrosine hydroxylase mediated regulation of dopamine synthesis.Journal of computational neuroscience · 2007Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study was undertaken to characterise the protein phosphatases in bovine adrenal chromaffin cells acting on tyrosine hydroxylase. Cells were pre-labelled with 32Pi and permeabilized with digitonin. The extent of dephosphorylation of Ser-8, Ser-19, Ser-31 and Ser-40 on tyrosine hydroxylase was found to be 30%, 38%, 37% and 71% respectively over 5 min. For Ser-19, Ser-31 and Ser-40 the dephosphorylation was entirely due to protein phosphatase 2A, as the dephosphorylation could be completely blocked by microcystin, but not by the protein phosphatase I inhibitory peptide. Permeabilization did not change the distribution of protein phosphatase 2A or tyrosine hydroxylase, or the activity of PP2A, from that occurring in intact cells. The dephosphorylation of Ser-8 was not altered by any inhibitor, suggesting the involvement of other protein phosphatases. The method developed here can be used to determine the protein phosphatases acting on substrates in conditions closely approximating those in situ, including the endogenous state of substrate phosphorylation and phosphatase location.
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