ArticleNature structural & molecular biology2008
The central unit within the 19S regulatory particle of the proteasome.
Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
65 citing papers in PubMed, 119 citations in OpenAlex.
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Regulation via compartmentation: adaptive localization of the proteasome under stress.Biochemical Society transactions · 2025Review
- CX26 promotes pancreatic cancer progression by competitively inhibiting interaction of c-Myc with PSMD2 and enhancing c-Myc stability.Journal of translational medicine · 2025Article
- The Unified Theory of Neurodegeneration Pathogenesis Based on Axon Deamidation.International journal of molecular sciences · 2025Review
- Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.Nature communications · 2025Article
- Primed for Interactions: Investigating the Primed Substrate Channel of the Proteasome for Improved Molecular Engagement.Molecules (Basel, Switzerland) · 2024Review
- Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024Review
- RACK1 facilitates breast cancer progression by competitively inhibiting the binding of β-catenin to PSMD2 and enhancing the stability of β-catenin.Cell death & disease · 2023Article
- How Viruses Use the VCP/p97 ATPase Molecular Machine.Viruses · 2021Review
- The prognostic value of USP14 and PSMD14 expression in non-small cell lung cancer.Annals of translational medicine · 2021Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Article
- Review
- Proteasome lid bridges mitochondrial stress with Cdc53/Cullin1 NEDDylation status.Redox biology · 2019Article
- The Arabidopsis MIEL1 E3 ligase negatively regulates ABA signalling by promoting protein turnover of MYB96.Nature communications · 2016Article
- Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases.BMB reports · 2016Review
- Monoubiquitination in proteasomal degradation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death.Cell research · 2016Review
- AFM Imaging Reveals Topographic Diversity of Wild Type and Z Variant Polymers of Human α1-Proteinase Inhibitor.PloS one · 2016Article
- Protein Folding and Mechanisms of Proteostasis.International journal of molecular sciences · 2015Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The 26S proteasome is a multisubunit enzyme composed of a cylindrical catalytic core (20S) and a regulatory particle (19S) that together perform the essential degradation of cellular proteins tagged by ubiquitin. To date, however, substrate trajectory within the complex remains elusive. Here we describe a previously unknown functional unit within the 19S, comprising two subunits, Rpn1 and Rpn2. These toroids physically link the site of substrate recruitment with the site of proteolysis. Rpn2 interfaces with the 20S, whereas Rpn1 sits atop Rpn2, serving as a docking site for a substrate-recruitment factor. The 19S ATPases encircle the Rpn1-Rpn2 stack, covering the remainder of the 20S surface. Both Rpn1-Rpn2 and the ATPases are required for substrate translocation and gating of the proteolytic channel. Similar pairing of units is found in unfoldases and nuclear transporters, exposing common features of these protein nanomachines.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.