ArticleJournal of the American Chemical Society2023
Avidity-Based Method for the Efficient Generation of Monoubiquitinated Recombinant Proteins.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Solution structure of mouse HBS1L/SKI7-specific UBA domain in complex with ubiquitin: Implications for stalled ribosome recognition.PloS one · 2026Article
- Ion channel inhibition by targeted recruitment of NEDD4-2 with divalent nanobodies.Nature communications · 2025Article
- Developing a process of lentivirus purification from recombinant fluids using peptide affinity ligands.Bioengineering & translational medicine · 2025Article
- Liquid-liquid phase separation of α-synuclein is highly sensitive to sequence complexity.Protein science : a publication of the Protein Society · 2024Article
- Structure-guided engineering enables E3 ligase-free and versatile protein ubiquitination via UBE2E1.Nature communications · 2024Article
- Phase Separation and Fibrillization of Human Annexin A7 Are Mediated by Its Proline-Rich Domain.Biochemistry · 2023Article
- ALS Variants of Annexin A11's Proline-Rich Domain Impair Its S100A6-Mediated Fibril Dissolution.ACS chemical neuroscience · 2023Article
- Reversible phase separation of ESCRT protein ALIX through tyrosine phosphorylation.Science advances · 2023Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Monoubiquitination of proteins governs diverse physiological processes, and its dysregulation is implicated in multiple pathologies. The difficulty of preparing sufficient material often complicates the biophysical studies of monoubiquitinated recombinant proteins. Here we describe a robust avidity-based method that overcomes this problem. As a proof-of-concept, we produced milligram quantities of two monoubiquitinated targets, Parkinson's protein α-synuclein and ESCRT-protein ALIX, using NEDD4-family E3 ligases. Monoubiquitination hotspots were identified by quantitative chemical proteomics. Using FRAP and dye-binding assays, we uncovered strikingly opposite effects of monoubiquitination on the phase separation and fibrillization properties of these two amyloidogenic proteins, reflecting differences in their intermolecular interactions, thereby providing unique insights into the impact of monoubiquitination on protein aggregation.
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Registered trials
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