ArticleStructure (London, England : 1993)2016
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 93 citations in OpenAlex.
- Structures of dynamic interactors at native proteasomes by PhIX-MS and cryo-electron microscopy.Molecular cell · 2026Article
- Review
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.The Journal of biological chemistry · 2026Article
- Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover.Nature communications · 2026Article
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.bioRxiv : the preprint server for biology · 2025Article
- UBQLN2 is necessary for UBE3A-mediated proteasomal degradation of the domesticated retroelement PEG10.Journal of cell science · 2025Article
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Structural basis of K11/K48-branched ubiquitin chain recognition by the human 26S proteasome.Nature communications · 2025Article
- Structural basis for the midnolin-proteasome pathway and its role in suppressing myeloma.Molecular cell · 2025Article
- An adaptive peptide-binding site in ubiquitin receptor hRpn13 revealed by structural studies.Nature communications · 2025Article
- The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome.Cell reports · 2025Article
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- HERC3 facilitates ERAD of select membrane proteins by recognizing membrane-spanning domains.The Journal of cell biology · 2024Article
- A structure-based designed small molecule depletes hRpn13Nature communications · 2024Article
- Article
- E6AP AZUL interaction with UBQLN1/2 in cells, condensates, and an AlphaFold-NMR integrated structure.Structure (London, England : 1993) · 2023Article
- Proteasome substrate receptors and their therapeutic potential.Trends in biochemical sciences · 2022Review
- HECT ubiquitin ligases as accessory proteins of the plant proteasome.Essays in biochemistry · 2022Article
- Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma.Nature communications · 2021Article
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6 authors at 3 institutions in 1 country.
Funding
Abstract
Three receptors (Rpn1/S2/PSMD2, Rpn10/S5a, Rpn13/Adrm1) in the proteasome bind substrates by interacting with conjugated ubiquitin chains and/or shuttle factors (Rad23/HR23, Dsk2/PLIC/ubiquilin, Ddi1) that carry ubiquitinated substrates to proteasomes. We solved the structure of two such receptors with their preferred shuttle factor, namely hRpn13(Pru):hPLIC2(UBL) and scRpn1 T1:scRad23(UBL). We find that ubiquitin folds in Rad23 and Dsk2 are fine-tuned by residue substitutions to achieve high affinity for Rpn1 and Rpn13, respectively. A single substitution in hPLIC2 yields enhanced interactions with the Rpn13 ubiquitin contact surface and sterically blocks hRpn13 binding to its preferred ubiquitin chain type, K48-linked chains. Rpn1 T1 binds two ubiquitins in tandem and we find that Rad23 binds exclusively to the higher-affinity Helix28/Helix30 site. Rad23 contacts at Helix28/Helix30 are optimized compared to ubiquitin by multiple conservative amino acid substitutions. Thus, shuttle factors deliver substrates to proteasomes through fine-tuned ubiquitin-like surfaces.
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