ArticleScientific reports2017
Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 46 citations in OpenAlex.
- The C-terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity.FEBS open bio · 2026Article
- Reconstitution of protein arginylation pathways in bacteria for robust identification and quantification.Communications biology · 2026Article
- Review
- Proteoform Catcher: The Power of 2D SDS-PAGE, Western Blotting, and Mass Spectrometry in Protein Characterization.Advances in experimental medicine and biology · 2026Article
- An unbiased proteomic platform for ATE1-based arginylation profiling.Nature chemical biology · 2025Article
- Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025Review
- Structure and Mechanism of Aminoacyl-tRNA-Protein L/F- and R-transferases.Journal of molecular biology · 2025Review
- Top-Down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.Analytical chemistry · 2025Article
- Arginylation of ⍺-tubulin at E77 regulates microtubule dynamics via MAP1S.The Journal of cell biology · 2025Article
- Identification of an Intrinsically Disordered Region (IDR) in Arginyltransferase 1 (ATE1).Biochemistry · 2024Article
- Posttranslational Modifications ofPharmacological reviews · 2024Review
- Identification of an intrinsically disordered region (IDR) in arginyltransferase 1 (ATE1).bioRxiv : the preprint server for biology · 2024Article
- Top-down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.bioRxiv : the preprint server for biology · 2024Article
- Oligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function.Nature communications · 2024Article
- The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.Nature communications · 2023Article
- Post-translational modifications of soluble α-synuclein regulate the amplification of pathological α-synuclein.Nature neuroscience · 2023Article
- Iron-sulfur clusters are involved in post-translational arginylation.Nature communications · 2023Article
- Article
- Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.Journal of molecular biology · 2022Review
- Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.Molecular and cellular biology · 2022Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Alpha synuclein (α-syn) is a central player in neurodegeneration, but the mechanisms triggering its pathology are not fully understood. Here we found that α-syn is a highly efficient substrate for arginyltransferase ATE1 and is arginylated in vivo by a novel mid-chain mechanism that targets the acidic side chains of E46 and E83. Lack of arginylation leads to increased α-syn aggregation and causes the formation of larger pathological aggregates in neurons, accompanied by impairments in its ability to be cleared via normal degradation pathways. In the mouse brain, lack of arginylation leads to an increase in α-syn's insoluble fraction, accompanied by behavioral changes characteristic for neurodegenerative pathology. Our data show that lack of arginylation in the brain leads to neurodegeneration, and suggests that α-syn arginylation can be a previously unknown factor that facilitates normal α-syn folding and function in vivo.
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Registered trials
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