ArticleThe Journal of biological chemistry2012
Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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The trial behind it
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Who cites it
75 citing papers in PubMed, 112 citations in OpenAlex.
- Safety, Pharmacokinetics, Translational and Molecular Mechanistic Insights on the Prostate Cancer Recurrence Suppressor Pseurotin A.Molecules (Basel, Switzerland) · 2025Article
- A chromosome-coupled ubiquitin-proteasome pathway is required for meiotic surveillance.Cell death and differentiation · 2024Article
- Domains in Action: Understanding Ddi1's Diverse Functions in the Ubiquitin-Proteasome System.International journal of molecular sciences · 2024Review
- Bidirectional substrate shuttling between the 26S proteasome and the Cdc48 ATPase promotes protein degradation.Molecular cell · 2024Article
- NSP6 inhibits the production of ACE2-containing exosomes to promote SARS-CoV-2 infectivity.mBio · 2024Article
- Mutation in the 26S proteasome regulatory subunitFrontiers in cellular and infection microbiology · 2024Article
- Article
- To Kill or to Be Killed: How Does the Battle between the UPS and Autophagy Maintain the Intracellular Homeostasis in Eukaryotes?International journal of molecular sciences · 2023Review
- Proteasome substrate receptors and their therapeutic potential.Trends in biochemical sciences · 2022Review
- RPNs Levels Are Prognostic and Diagnostic Markers for Hepatocellular Carcinoma.Journal of oncology · 2022Article
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- Proteasome in action: substrate degradation by the 26S proteasome.Biochemical Society transactions · 2021Review
- The ubiquitin-proteasome system in regulation of the skeletal muscle homeostasis and atrophy: from basic science to disorders.The journal of physiological sciences : JPS · 2020Review
- Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome.Biomolecules · 2020Review
- Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy.Molecules (Basel, Switzerland) · 2020Review
- Ubiquitin-proteasome-mediated cyclin C degradation promotes cell survival following nitrogen starvation.Molecular biology of the cell · 2020Article
- Proteomic mapping of Drosophila transgenic elav.L-GAL4/+ brain as a tool to illuminate neuropathology mechanisms.Scientific reports · 2020Article
- The nutrient sensor OGT regulates Hipk stability and tumorigenic-like activities inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates.Nature communications · 2020Article
- Differential toxicity of ataxin-3 isoforms in Drosophila models of Spinocerebellar Ataxia Type 3.Neurobiology of disease · 2019Article
15 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
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Substrates tagged with (poly)ubiquitin for degradation can be targeted directly to the 26 S proteasome where they are proteolyzed. Independently, ubiquitin conjugates may also be delivered by bivalent shuttles. The majority of shuttles attach to the proteasome through a ubiquitin-like domain (UBL) while anchoring cargo at a C-terminal polyubiquitin-binding domain(s). We found that two shuttles of this class, Rad23 and Dsk2, dock at two different receptor sites embedded within a single subunit of the 19 S proteasome regulatory particle, Rpn1. Their association/dissociation constants and affinities for Rpn1 are similar. In contrast, another UBL-containing protein, the deubiquitinase Ubp6, is also anchored by Rpn1, yet it dissociates slower, thus behaving as an occasional proteasome subunit that is distinct from the transiently associated shuttles. Two neighboring subunits, Rpn10 and Rpn13, show a marked preference for polyubiquitin over UBLs. Rpn10 attaches to the central solenoid portion of Rpn1, although this association is stabilized by the presence of a third subunit, Rpn2. Rpn13 binds directly to Rpn2. These intrinsic polyubiquitin receptors may compete with substrate shuttles for their polyubiquitin-conjugate cargos, thereby aiding release of the emptied shuttles. By binding multiple ubiquitin-processing factors simultaneously, Rpn1 is uniquely suited to coordinate substrate recruitment, deubiquitination, and movement toward the catalytic core. The broad range of affinities for ubiquitin, ubiquitin-like, and non-ubiquitin signals by adjacent yet nonoverlapping sites all within the base represents a hub of activity that coordinates the intricate relay of substrates within the proteasome, and consequently it influences substrate residency time and commitment to degradation.
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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.