ArticleNature communications2016
Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.
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Who cites it
23 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Review
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.The Journal of biological chemistry · 2026Article
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.bioRxiv : the preprint server for biology · 2025Article
- Molecular exaptation by the integrin αI domain.Science advances · 2025Article
- Article
- Proximal Co-Translation Facilitates Detection of Weak Protein-Protein Interactions.International journal of molecular sciences · 2024Article
- DNA damage-induced proteasome phosphorylation controls substrate recognition and facilitates DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Proteasome substrate receptors and their therapeutic potential.Trends in biochemical sciences · 2022Review
- Split-Chloramphenicol Acetyl Transferase Assay to Study Protein-Protein Interactions and Ubiquitylation inBio-protocol · 2022Article
- Site-specific ubiquitination: Deconstructing the degradation tag.Current opinion in structural biology · 2022Review
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- Deubiquitylating enzymes in neuronal health and disease.Cell death & disease · 2021Review
- Proteasome Biology: Chemistry and Bioengineering Insights.Polymers · 2020Review
- Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy.Molecules (Basel, Switzerland) · 2020Review
- Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10.Nature communications · 2020Article
- Remodeling Membrane Binding by Mono-Ubiquitylation.Biomolecules · 2019Article
- Non-Proteasomal UbL-UbA Family of Proteins in Neurodegeneration.International journal of molecular sciences · 2019Review
- Structure of hRpn10 Bound to UBQLN2 UBL Illustrates Basis for Complementarity between Shuttle Factors and Substrates at the Proteasome.Journal of molecular biology · 2019Article
- Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms.Frontiers in molecular biosciences · 2019Review
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin receptors decode ubiquitin signals into many cellular responses. Ubiquitin receptors also undergo coupled monoubiquitylation, and rapid deubiquitylation has hampered the characterization of the ubiquitylated state. Using bacteria that express a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state. The structure shows a novel ubiquitin-binding patch that directs K84 ubiquitylation. Superimposition of ubiquitylated-Rpn10 onto electron-microscopy models of proteasomes indicates that the Rpn10-conjugated ubiquitin clashes with Rpn9, suggesting that ubiquitylation might be involved in releasing Rpn10 from the proteasome. Indeed, ubiquitylation on immobilized proteasomes dissociates the modified Rpn10 from the complex, while unmodified Rpn10 mainly remains associated. In vivo experiments indicate that contrary to wild type, Rpn10-K84R is stably associated with the proteasomal subunit Rpn9. Similarly Rpn10, but not ubiquitylated-Rpn10, binds Rpn9 in vitro. Thus we suggest that ubiquitylation functions to dissociate modified ubiquitin receptors from their targets, a function that promotes cyclic activity of ubiquitin receptors.
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