ArticleInternational journal of molecular sciences2021
α-Synuclein A53T Binds to Transcriptional Adapter 2-Alpha and Blocks Histone H3 Acetylation.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- A split biotin ligase approach reveals proteins associated with oligomeric alpha-synuclein during aggregation.Scientific reports · 2026Article
- Proximity labeling in neuroscience: decoding molecular landscapes for precision neurology.Translational neurodegeneration · 2026Review
- A Split Biotin Ligase Approach to Revealing Proteins Associated with Oligomeric Alpha-Synuclein During Aggregation.Research square · 2025Article
- Review
- Review
- Epigenetics Modulators as Therapeutics for Neurological Disorders.Current pharmaceutical design · 2025Review
- Further screening of SNP loci of eggshell translucency related genes and evaluation of genetic effects.Poultry science · 2024Article
- Inhibition of EHMT1/2 rescues synaptic damage and motor impairment in a PD mouse model.Cellular and molecular life sciences : CMLS · 2024Article
- Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson's Disease.International journal of molecular sciences · 2023Review
- α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies.Neural regeneration research · 2023Article
- Unraveling the Complex Interplay between Alpha-Synuclein and Epigenetic Modification.International journal of molecular sciences · 2023Review
- Hypoxic stress accelerates the propagation of pathological alpha-synuclein and degeneration of dopaminergic neurons.CNS neuroscience & therapeutics · 2023Article
- Increased Levels of the Parkinson's Disease-Associated Gene ITPKB Correlate with Higher Expression Levels of α-Synuclein, Independent of Mutation Status.International journal of molecular sciences · 2023Article
- α-Synuclein and Mechanisms of Epigenetic Regulation.Brain sciences · 2023Review
- Epigenetic modification in Parkinson's disease.Frontiers in cell and developmental biology · 2023Review
- Deciphering Spatial Protein-Protein Interactions in Brain Using Proximity Labeling.Molecular & cellular proteomics : MCP · 2022Review
- A Plasma Circular RNA Profile Differentiates Subjects with Alzheimer's Disease and Mild Cognitive Impairment from Healthy Controls.International journal of molecular sciences · 2022Article
- Alpha-synuclein supports type 1 interferon signalling in neurons and brain tissue.Brain : a journal of neurology · 2022Article
- α-Synuclein at the Presynaptic Axon Terminal as a Double-Edged Sword.Biomolecules · 2022Review
- Histone deacetylase inhibitor attenuates intestinal mucosal injury in fatally scalded rats.Annals of translational medicine · 2022Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
α-Synuclein (α-syn) is a hallmark amyloidogenic protein component of Lewy bodies in dopaminergic neurons affected by Parkinson's disease (PD). Despite the multi-faceted gene regulation of α-syn in the nucleus, the mechanism underlying α-syn crosstalk in chromatin remodeling in PD pathogenesis remains elusive. Here, we identified transcriptional adapter 2-alpha (TADA2a) as a novel binding partner of α-syn using the BioID system. TADA2a is a component of the p300/CBP-associated factor and is related to histone H3/H4 acetylation. We found that α-syn A53T was more preferentially localized in the nucleus than the α-syn wild-type (WT), leading to a stronger disturbance of TADA2a. Indeed, α-syn A53T significantly reduced the level of histone H3 acetylation in SH-SY5Y cells; its reduction was also evident in the striatum (STR) and substantia nigra (SN) of mice that were stereotaxically injected with α-syn preformed fibrils (PFFs). Interestingly, α-syn PFF injection resulted in a decrease in TADA2a in the STR and SN of α-syn PFF-injected mice. Furthermore, the levels of TADA2a and acetylated histone H3 were significantly decreased in the SN of patients with PD. Therefore, histone modification through α-syn A53T-TADA2a interaction may be associated with α-syn-mediated neurotoxicity in PD pathology.
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