ArticleNature communications2011
Rad23 escapes degradation because it lacks a proteasome initiation region.
Article in Nature communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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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.
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Who cites it
65 citing papers in PubMed.
- 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
- Molecular features defining the efficiency of bioPROTACs.Communications biology · 2025Article
- A kinetic model for USP14 regulated substrate degradation in 26S proteasome.PLoS computational biology · 2025Article
- An mRNA Vaccine for Herpes Zoster and Its Efficacy Evaluation in Naïve/Primed Murine Models.Vaccines · 2025Article
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- Ubiquitin-Independent Degradation: An Emerging PROTAC Approach?BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The role of ubiquitination in health and disease.MedComm · 2024Review
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Article
- A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases.Journal of molecular biology · 2023Article
- Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.Cellular and molecular life sciences : CMLS · 2023Article
- The Ufd1 cofactor determines the linkage specificity of polyubiquitin chain engagement by the AAA+ ATPase Cdc48.Molecular cell · 2023Article
- 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
- Ubiquitin modulates 26Science advances · 2022Article
- Degron masking outlines degronons, co-degrading functional modules in the proteome.Communications biology · 2022Article
- Design principles that protect the proteasome from self-destruction.Protein science : a publication of the Protein Society · 2022Article
- How Viruses Use the VCP/p97 ATPase Molecular Machine.Viruses · 2021Review
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- HPE1, an Effector from Zebra Chip Pathogen Interacts with Tomato Proteins and Perturbs Ubiquitinated Protein Accumulation.International journal of molecular sciences · 2021Article
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
5 authors.
Funding
Abstract
Rad23 is an adaptor protein that binds to both ubiquitinated substrates and to the proteasome. Despite its association with the proteasome, Rad23 escapes degradation. Here we show that Rad23 remains stable because it lacks an effective initiation region at which the proteasome can engage the protein and unfold it. Rad23 contains several internal, unstructured loops, but these are too short to act as initiation regions. Experiments with model proteins show that internal loops must be surprisingly long to engage the proteasome and support degradation. These length requirements are not specific to Rad23 and reflect a general property of the proteasome.
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Registered trials
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