ArticleMolecular biology of the cell2007
Inhibition of the ubiquitin-proteasome system induces stress granule formation.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 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.
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Who cites it
156 citing papers in PubMed, 244 citations in OpenAlex.
- Stress granules at the crossroads of the proteostasis network.RNA biology · 2026Review
- GCN2 in proteostasis: structural logic, signalling networks and disease.The FEBS journal · 2026Review
- TSC2 is a stress granule suppressor.bioRxiv : the preprint server for biology · 2026Article
- Enhancement of Therapeutic mRNA Translation in Cellular Stress Conditions.International journal of molecular sciences · 2026Review
- Contrastive learning of dynamic processing body formation reveals undefined mechanisms of approved compounds.iScience · 2026Article
- Stress-specific NONO interactomes reveal a key role of Hsp70 chaperone activity in regulation of paraspeckle formation.Journal of cell science · 2026Article
- Unveiling prognostic genes and regulatory mechanisms of stress granules in gastric cancers: an integrated analysis of bulk transcriptomics and single-cell RNA sequencing.Frontiers in oncology · 2026Article
- Correlative Raman and immunofluorescence imaging reveals different protein abundance between stress granules induced by oxidative damage.Journal of inorganic biochemistry · 2026Article
- NEDD8, stress granules, and amyotrophic lateral sclerosis: unveiling the therapeutic potential of the NEDP1 protease.Essays in biochemistry · 2025Review
- TBK1 is a signaling hub in coordinating stress-adaptive mechanisms in head and neck cancer progression.Autophagy · 2025Article
- Regulation of physiological and pathological condensates by molecular chaperones.The FEBS journal · 2025Review
- Selective Translation Under Heat Shock: Integrating HSP70 mRNA Regulation with Cellular Stress Responses in Yeast and Mammals.Molecular biology of the cell · 2025Review
- The integrated stress response in neurodegenerative diseases.Molecular neurodegeneration · 2025Review
- Proteasome caspase-like activity regulates stress granules and proteasome condensates.Frontiers in cell and developmental biology · 2025Article
- Dynamic composition of stress granules in Trypanosoma brucei.PLoS pathogens · 2024Article
- Sodium arsenite induces aggresome formation by promoting PICK1 BAR domain homodimer formation.Molecular biology of the cell · 2024Article
- Pifithrin-µ Induces Stress Granule Formation, Regulates Cell Survival, and Rewires Cellular Signaling.Cells · 2024Article
- Protein-rich foods, sea foods, and gut microbiota amplify immune responses in chronic diseases and cancers - Targeting PERK as a novel therapeutic strategy for chronic inflammatory diseases, neurodegenerative disorders, and cancer.Pharmacology & therapeutics · 2024Review
- ALS' Perfect Storm:Cells · 2024Review
- RNA in axons, dendrites, synapses and beyond.Frontiers in molecular neuroscience · 2024Review
96 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 inhibition of the ubiquitin-dependent proteasome system (UPS) via specific drugs is one type of approach used to combat cancer. Although it has been suggested that UPS inhibition prevents the rapid decay of AU-rich element (ARE)-containing messages, very little is known about the cellular mechanisms leading to this effect. Here we establish a link between the inhibition of UPS activity, the formation of cytoplasmic stress granules (SGs), and mRNA metabolism. The assembly of the SGs requires the phosphorylation of the translation initiation factor eIF2alpha by a mechanism involving the stress kinase GCN2. On prolonged UPS inhibition and despite the maintenance of eIF2alpha phosphorylation, SGs disassemble and translation recovers in an Hsp72 protein-dependent manner. The formation of these SGs coincides with the disassembly of processing bodies (PBs), known as mRNA decay entities. As soon as the SGs assemble, they recruit ARE-containing messages such as p21(cip1) mRNA, which are stabilized under these conditions. Hence, our findings suggest that SGs could be considered as one of the players that mediate the early response of the cell to proteasome inhibitors by interfering temporarily with mRNA decay pathways.
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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.