ArticleThe Journal of biological chemistry2010
Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- The structure and function of deubiquitinases: lessons from budding yeast.Open biology · 2020Review
- Catalytically Active Proteasomes Function Predominantly in the Cytosol.The Journal of biological chemistry · 2016Article
- Base-CP proteasome can serve as a platform for stepwise lid formation.Bioscience reports · 2015Article
- Conformational switching of the 26S proteasome enables substrate degradation.Nature structural & molecular biology · 2013Article
- Article
- Near-atomic resolution structural model of the yeast 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress.Journal of molecular biology · 2011Article
- Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1.BMC biology · 2011Article
- Sts1 plays a key role in targeting proteasomes to the nucleus.The Journal of biological chemistry · 2011Article
- Synthetic lethality of rpn11-1 rpn10Δ is linked to altered proteasome assembly and activity.Current genetics · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
A major fraction of intracellular protein degradation is mediated by the proteasome. Successful degradation of these substrates requires ubiquitination and delivery to the proteasome followed by protein unfolding and disassembly of the multiubiquitin chain. Enzymes, such as Rpn11, dismantle multiubiquitin chains, and mutations can affect proteasome assembly and activity. We report that different rpn11 mutations can affect proteasome interaction with ubiquitinated proteins. Moreover, proteasomes are unstable in rpn11-1 and do not form productive interactions with multiubiquitinated proteins despite high levels in cell extracts. However, increased levels of ubiquitinated proteins were found associated with shuttle factors. In contrast to rpn11-1, proteasomes expressing a catalytically inactive mutant (rpn11(AXA)) were more stable and bound very high amounts of ubiquitinated substrates. Expression of the carboxyl-terminal domain of Rpn11 partially suppressed the growth and proteasome stability defects of rpn11-1. These results indicate that ubiquitinated substrates are preferentially delivered to intact proteasome.
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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.