ArticleMolecular cell2014
An inducible chaperone adapts proteasome assembly to stress.
Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
43 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Article
- Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.Nature communications · 2025Article
- Structural basis of human 20S proteasome biogenesis.Nature communications · 2024Article
- Proteasome gene expression is controlled by coordinated functions of multiple transcription factors.The Journal of cell biology · 2024Article
- Decoding the Cellular Trafficking of Prion-like Proteins in Neurodegenerative Diseases.Neuroscience bulletin · 2024Review
- Riboproteome remodeling during quiescence exit iniScience · 2024Article
- Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis.Biomolecules · 2023Review
- Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.The Journal of biological chemistry · 2023Article
- Proteasome granule formation is regulated through mitochondrial respiration and kinase signaling.Journal of cell science · 2022Article
- Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones.Cell reports · 2022Article
- Effects of mTORC1 inhibition on proteasome activity and levels.BMB reports · 2022Article
- Slt2 Is Required to Activate ER-Stress-Protective Mechanisms through TORC1 Inhibition and Hexosamine Pathway Activation.Journal of fungi (Basel, Switzerland) · 2022Article
- Yeast Nst1 is a novel component of P-bodies and is a specific suppressor of proteasome base assembly defects.Molecular biology of the cell · 2021Article
- Proteomic analysis revealed the roles of YRR1 deletion in enhancing the vanillin resistance of Saccharomyces cerevisiae.Microbial cell factories · 2021Article
- Corilagin induces human glioblastoma U251 cell apoptosis by impeding activity of (immuno)proteasome.Oncology reports · 2021Article
- Mutant thermal proteome profiling for characterization of missense protein variants and their associated phenotypes within the proteome.The Journal of biological chemistry · 2020Article
- Proteomic analysis of affinity-purified 26S proteasomes identifies a suite of assembly chaperones inThe Journal of biological chemistry · 2019Article
- Two alternative mechanisms regulate the onset of chaperone-mediated assembly of the proteasomal ATPases.The Journal of biological chemistry · 2019Article
- Article
Corrections and comments
- Commented on by
Authors and funding
6 authors.
Funding
Abstract
The proteasome is essential for the selective degradation of most cellular proteins. To survive overwhelming demands on the proteasome arising during environmental stresses, cells increase proteasome abundance. Proteasome assembly is known to be complex. How stressed cells overcome this vital challenge is unknown. In an unbiased suppressor screen aimed at rescuing the defects of a yeast Rpt6 thermosensitive proteasome mutant, we identified a protein, hereafter named Adc17, as it functions as an ATPase dedicated chaperone. Adc17 interacts with the amino terminus of Rpt6 to assist formation of the Rpt6-Rpt3 ATPase pair, an early step in proteasome assembly. Adc17 is important for cell fitness, and its absence aggravates proteasome defects. The abundance of Adc17 increases upon proteasome stresses, and its function is crucial to maintain homeostatic proteasome levels. Thus, cells have mechanisms to adjust proteasome assembly when demands increase, and Adc17 is a critical effector of this process.
Indexed as
Identifiers
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.