ArticleNAR molecular medicine2024
ATM-mediated co-chaperone DNAJB11 phosphorylation facilitates α-synuclein folding upon DNA double-stranded breaks.
Article in NAR molecular medicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Leveraging learned representations and multitask learning for lysine methylation site discovery.Scientific reports · 2026Article
- Leveraging learned representations and multitask learning for lysine methylation site discovery.bioRxiv : the preprint server for biology · 2025Article
- DNA Damage Response Regulation Alleviates Neuroinflammation in a Mouse Model of α-Synucleinopathy.Biomolecules · 2025Article
- EGFR phosphorylates DNAJB1 to suppress α-synuclein aggregation in Parkinson's disease.NPJ Parkinson's disease · 2025Article
- Alpha-synuclein modulates the repair of genomic DNA double-strand breaks in a DNA-PKNeurobiology of disease · 2024Article
- Polo-like kinase inhibition leads to neuroprotection of neurons bearing alpha-synuclein Lewy body-like inclusionsmicroPublication biology · 2024Article
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Authors and funding
6 authors.
Funding
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Abstract
Parkinson's disease (PD) is a prevalent neurodegenerative disorder marked by the pathological accumulation of α-synuclein aggregates in dopaminergic neurons. This α-synuclein dyshomeostasis is caused by an interplay between aging, genetic and environmental factors. Aging process-related DNA damage and impaired DNA repair have recently been observed in the PD process. However, the precise neuronal response to DNA damage in PD remains largely unknown. Here, we demonstrate that double-strand breaks (DSBs) induce α-synuclein aggregation. Analysis of a large-scale proteomic analysis of ATM and ATR substrates identified a potential candidate in the HSP70 folding system responding to DNA damage. ATM phosphorylates co-chaperone DNAJB11 at threonine 188 which specifically facilitates the delivery of misfolded α-synuclein, but not tau or transthyretin protein, to the HSP70 folding system upon DSBs. Alteration of this response impairs the neurite outgrowth. Remarkably, DNAJB11 threonine 188 phosphorylation correlates with disease severity in transgenic
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Registered trials
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