ArticleMolecular cell2024
eIF4F complex dynamics are important for the activation of the integrated stress response.
Article in Molecular cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Heat stress promotes pre-tRNA capping to modulate cap-dependent translation in Saccharomyces cerevisiae.Nature communications · 2026Article
- Thermosensitivity of cellular translation restricts the growth of fission yeast at high temperatures.Communications biology · 2026Article
- Peptide antibody tools to dissect specific functions of eIF4A paralogs in cancer.Discover oncology · 2025Article
- Targeting eIF4A with RNA Aptamers Enhances Salt Stress Tolerance in Rice Through Modulation of Translation Initiation.Rice (New York, N.Y.) · 2025Article
- Insights into the role of collided ribosomes during the activation of the integrated stress response.Biochemical Society transactions · 2025Review
- Hog1/p38 regulates the integrated stress response (ISR) and global transcriptomic changes inbioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
In response to stress, eukaryotes activate the integrated stress response (ISR) via phosphorylation of eIF2α to promote the translation of pro-survival effector genes, such as GCN4 in yeast. Complementing the ISR is the target of rapamycin (TOR) pathway, which regulates eIF4E function. Here, we probe translational control in the absence of eIF4E in Saccharomyces cerevisiae. Intriguingly, we find that loss of eIF4E leads to de-repression of GCN4 translation. In addition, we find that de-repression of GCN4 translation is accompanied by neither eIF2α phosphorylation nor reduction in initiator ternary complex (TC). Our data suggest that when eIF4E levels are depleted, GCN4 translation is de-repressed via a unique mechanism that may involve faster scanning by the small ribosome subunit due to increased local concentration of eIF4A. Overall, our findings suggest that relative levels of eIF4F components are key to ribosome dynamics and may play important roles in translational control of gene expression.
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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.