ArticleNeurochemical research2015
Protein phosphatase 2A is involved in the tyrosine hydroxylase phosphorylation regulated by α-synuclein.
Article in Neurochemical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.
- Network Analysis Identifies Disease-Specific Pathways for Parkinson's Disease.Molecular neurobiology · 2018Pooled it
- Glycyrrhizic acid combined with human adipose-derived MSCs synergistically alleviates the MPP+/MPTP-induced parkinson's disease by inducing autophagy through PI3K/AKT/HIF-1α pathway.Stem cell research & therapy · 2025Article
- Neuroprotective efficacy of berberine and caffeine against rotenone-induced neuroinflammatory and oxidative disturbances associated with Parkinson's disease via inhibiting α-synuclein aggregation and boosting dopamine release.Inflammopharmacology · 2025Article
- Galangin reduces MPTP-induced dopamine neuron injury via the autophagy dependent-PI3K/AKT pathway.Frontiers in aging neuroscience · 2025Article
- Cancerous Inhibitor of Protein Phosphatase 2A (CIP2A): Could It Be a Promising Biomarker and Therapeutic Target in Parkinson's Disease?Molecular neurobiology · 2022Article
- Enhanced tyrosine hydroxylase activity induces oxidative stress, causes accumulation of autotoxic catecholamine metabolites, and augments amphetamine effects in vivo.Journal of neurochemistry · 2021Article
- Copper Dependent Modulation of α-Synuclein Phosphorylation in Differentiated SHSY5Y Neuroblastoma Cells.International journal of molecular sciences · 2021Article
- "Janus-Faced" α-Synuclein: Role in Parkinson's Disease.Frontiers in cell and developmental biology · 2021Review
- PP2A and Its Inhibitors in Helper T-Cell Differentiation and Autoimmunity.Frontiers in immunology · 2021Review
- NT5DC2 affects the phosphorylation of tyrosine hydroxylase regulating its catalytic activity.Journal of neural transmission (Vienna, Austria : 1996) · 2020Article
- Protein phosphatase 2A as a therapeutic target in inflammation and neurodegeneration.Pharmacology & therapeutics · 2019Review
- Evaluation of α-synuclein and apolipoprotein E as potential biomarkers in cerebrospinal fluid to monitor pharmacotherapeutic efficacy in dopamine dictated disease states of Parkinson's disease and schizophrenia.Neuropsychiatric disease and treatment · 2019Article
- Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.F1000Research · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Synuclein (α-Syn) plays a crucial role in the pathophysiology of Parkinson's disease (PD), the degeneration of dopaminergic neurons. Previous studies have shown that α-Syn regulates dopamine synthesis by binding to and inhibiting tyrosine hydroxylase (TH). In neurons, protein phosphatases (PPs) play a prominent role in directing signaling toward survival or degeneration. This study was to re-evaluate whether α-Syn could regulate the tyrosine hydroxylase phosphorylation by protein phosphatase-2A (PP2A) in dopaminergic MN9D cells and cortex neurons. Our data demonstrated for the first time that α-Syn stimulates PP2A activity and reduces phosphorylation of TH through regulating the methylation of PP2A in dopaminergic MN9D cells and primary cortex neurons. Increased PP2A activity and reduced phosphorylation of PP2A at Y307 (inactive form of PP2A) were observed in α-Syn overexpression dopaminergic cells (Syn) and primary cortex neurons, and the TH phosphorylation relieved by enhancing PP2A methylation in Syn group could be abated by using PP inhibitors, okadaic acid (OKA). OKA could reduce the cell damage and cell apoptosis induced by α-Syn. Thus our findings may provide an insight into the complicated pathogenesis of PD as well as some clues to the development of novel therapeutic strategies targeting at PP2A.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.