ArticleCell reports2020
Protein Stability Buffers the Cost of Translation Attenuation following eIF2α Phosphorylation.
Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- NAC promotes co-translational protein folding at the ribosomal tunnel exit.Molecular cell · 2026Article
- Termination of the integrated stress response.Science (New York, N.Y.) · 2026Article
- Space radiation induces distinct senescent phenotypes: Implications for space travel.npj aging · 2025Article
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- Ageing-related decline of translation as a consequence of transcription dysregulation.Journal of the Royal Society, Interface · 2025Article
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- Cellular resiliency and survival of Neuro-2a cells under extreme stress.Experimental cell research · 2024Article
- Article
- Effects of Individual Essential Amino Acids on Growth Rates of Young Rats Fed a Low-Protein Diet.Animals : an open access journal from MDPI · 2024Article
- Sustained OMA1-mediated integrated stress response is beneficial for spastic ataxia type 5.Brain : a journal of neurology · 2024Article
- Mitochondrial aminoacyl-tRNA synthetases trigger unique compensatory mechanisms in neurons.Human molecular genetics · 2024Article
- Mitochondrial Quality Control via Mitochondrial Unfolded Protein Response (mtUPR) in Ageing and Neurodegenerative Diseases.Biomolecules · 2023Review
- Monosomes buffer translational stress to allow for active ribosome elongation.Frontiers in molecular biosciences · 2023Article
- Adaptation to chronic ER stress enforces pancreatic β-cell plasticity.Nature communications · 2022Article
- Cellular responses to halofuginone reveal a vulnerability of the GCN2 branch of the integrated stress response.The EMBO journal · 2022Article
- An Overview of Methods for Detecting eIF2α Phosphorylation and the Integrated Stress Response.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Anota2seq Analysis for Transcriptome-Wide Studies of mRNA Translation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.International journal of molecular sciences · 2021Review
- Substrate recognition determinants of human eIF2α phosphatases.Open biology · 2021Article
- Stress Granules in the Post-transcriptional Regulation of Immune Cells.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Phosphorylation of the translation initiation factor eIF2α is a rapid and vital response to many forms of stress, including protein-misfolding stress in the endoplasmic reticulum (ER stress). It is believed to cause a general reduction in protein synthesis while enabling translation of few transcripts. Such a reduction of protein synthesis comes with the threat of depleting essential proteins, a risk thought to be mitigated by its transient nature. Here, we find that translation attenuation is not uniform, with cytosolic and mitochondrial ribosomal subunits being prominently downregulated. Translation attenuation of these targets persists after translation recovery. Surprisingly, this occurs without a measurable decrease in ribosomal proteins. Explaining this conundrum, translation attenuation preferentially targets long-lived proteins, a finding not only demonstrated by ribosomal proteins but also observed at a global level. This shows that protein stability buffers the cost of translational attenuation, establishing an evolutionary principle of cellular robustness.
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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.