ArticleStructure (London, England : 1993)2020
An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure.
Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 34 citations in OpenAlex.
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.The Journal of biological chemistry · 2026Article
- Proteasome activity maintains cell-type-specific gene expression.Cell reports · 2026Article
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.bioRxiv : the preprint server for biology · 2025Article
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- In-situ cross-linking mass spectrometry reveals compartment-specific proteasomal interactions and structural heterogeneity.Nature communications · 2025Article
- Structural basis of K11/K48-branched ubiquitin chain recognition by the human 26S proteasome.Nature communications · 2025Article
- NMR-Guided Studies to Establish the Binding Interaction between a Peptoid and Protein.Journal of the American Chemical Society · 2025Article
- An adaptive peptide-binding site in ubiquitin receptor hRpn13 revealed by structural studies.Nature communications · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- A structure-based designed small molecule depletes hRpn13Nature communications · 2024Article
- hRpn13 shapes the proteome and transcriptome through epigenetic factors HDAC8, PADI4, and transcription factor NF-κB p50.Molecular cell · 2024Article
- Chemical Synthesis of Non-hydrolyzable Ubiquitin(-Like) Hybrid Chains.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Proteasome substrate receptors and their therapeutic potential.Trends in biochemical sciences · 2022Review
- Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma.Nature communications · 2021Article
- Article
- Proteasome Inhibition Is an Effective Treatment Strategy for Microsporidia Infection in Honey Bees.Biomolecules · 2021Article
- Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2.Molecular cell · 2021Article
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021Review
- Article
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4 authors at 3 institutions in 1 country.
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Abstract
Rpn13/Adrm1 is recruited to the proteasome by PSMD1/Rpn2, where it serves as a substrate receptor that binds preferentially to K48-linked ubiquitin chains, an established signal for protein proteolysis. Here, we use NMR to solve the structure of hRpn13 Pru:hRpn2 (940-953):K48-diubiquitin. Surprisingly, hRpn2-bound hRpn13 selects a dynamic, extended conformation of K48-diubiquitin that is unique from previously determined structures. NMR experiments on free K48-diubiquitin demonstrate the presence of the reported "closed" conformation observed by crystallography, but also this more extended state, in which the hRpn13-binding surface is exposed. This extended K48-diubiquitin conformation is defined by interactions between L73 from G76-linked (distal) ubiquitin and a Y59-centered surface of K48-linked (proximal) ubiquitin. Furthermore, hRpn13 exchanges between the two ubiquitins within 100 ms, although prefers the proximal ubiquitin due to interactions with the K48 linker region. Altogether, these data lead to a revised model of how ubiquitinated substrates interact with the proteasome.
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