ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Light-Activatable Ubiquitin for Studying Linkage-Specific Ubiquitin Chain Formation Kinetics.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A Noncanonical Protein Degradation Pathway That Regulates Germ Cell Maintenance.Cell proliferation · 2026Article
- Use of a High-Affinity Ubiquitin-Binding Domain to Detect and Purify Ubiquitinated Substrates and Their Interacting Proteins.Bio-protocol · 2025Article
- Emerging tools and methods to study cell signalling mediated by branched ubiquitin chains.Biochemical Society transactions · 2025Review
- From exposure to innovation: decoding aromatic amines' role in bladder cancer mechanisms.Discover oncology · 2025Article
- Light-Activatable Ubiquitin for Studying Linkage-Specific Ubiquitin Chain Formation Kinetics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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Authors and funding
8 authors.
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Abstract
Ubiquitination is a dynamic post-translational modification governing protein abundance, function, and localization in eukaryotes. The Ubiquitin protein is conjugated to lysine residues of target proteins, but can also repeatedly be ubiquitinated itself, giving rise to a complex code of ubiquitin chains with different linkage types. To enable studying the cellular dynamics of linkage-specific ubiquitination, light-activatable polyubiquitin chain formation is reported here. By incorporating a photocaged lysine at specific sites within ubiquitin through amber codon suppression, light-dependent activation of ubiquitin chain extension is enabled for the monitoring of linkage-specific polyubiquitination. The studies reveal rapid, minute-scale ubiquitination kinetics for K11, K48, and K63 linkages. The role of individual components of the ubiquitin-proteasome system in K48-initiated chain synthesis is further studied by small molecule inhibition. The approach expands current perturbation strategies with the ability to control linkage-specific ubiquitination with high temporal resolution and should find broad application for studying ubiquitinome dynamics.
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Registered trials
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