ArticleeLife2014
A stress assembly that confers cell viability by preserving ERES components during amino-acid starvation.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.
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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
59 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024Pooled it
- Tissue-selective COPII modulator SEC16B aggravates cardiovascular disease by promoting lipid export.The EMBO journal · 2026Article
- Review
- Endoplasmic reticulum and Golgi stress signaling-mediated regulation of protein secretion.Cellular & molecular biology letters · 2026Review
- Phase separation and the tumor microenvironment.Cell communication and signaling : CCS · 2026Review
- Towards a unified framework for the function of endoplasmic reticulum exit sites.Nature reviews. Molecular cell biology · 2025Review
- Analysis of native Ist1 dynamics reveals multiple pools of ESCRT-III on endosomes.The Journal of cell biology · 2025Article
- The disruption of COPII vesicles activates HSF-1 through SEC-23.Journal of molecular cell biology · 2025Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- The formation of chaperone-rich GET bodies depends on the tetratricopeptide repeat region of Sgt2 and is reversed by NADH.Journal of cell science · 2025Article
- Composition and liquid-to-solid maturation of protein aggregates contribute to bacterial dormancy development and recovery.Nature communications · 2025Article
- Crosstalk Between Phase-Separated Membraneless Condensates and Membrane-Bound Organelles in Cellular Function and Disease.Advances in experimental medicine and biology · 2025Review
- The role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.EMBO reports · 2025Article
- Interplay between membranes and biomolecular condensates in the regulation of membrane-associated cellular processes.Experimental & molecular medicine · 2024Review
- TDP43 aggregation at ER-exit sites impairs ER-to-Golgi transport.Nature communications · 2024Article
- Remodeling of the secretory pathway is coordinated withiScience · 2024Article
- Tailored assemblies of COPII proteins in secretion.The Journal of cell biology · 2024Review
- Atg8/LC3 controls systemic nutrient surplus signaling in flies and humans.Current biology : CB · 2024Article
- TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport.Molecular biology of the cell · 2024Article
- The role of ER exit sites in maintaining P-body organization and transmitting ER stress response duringbioRxiv : the preprint server for biology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nutritional restriction leads to protein translation attenuation that results in the storage and degradation of free mRNAs in cytoplasmic assemblies. In this study, we show in Drosophila S2 cells that amino-acid starvation also leads to the inhibition of another major anabolic pathway, the protein transport through the secretory pathway, and to the formation of a novel reversible non-membrane bound stress assembly, the Sec body that incorporates components of the ER exit sites. Sec body formation does not depend on membrane traffic in the early secretory pathway, yet requires both Sec23 and Sec24AB. Sec bodies have liquid droplet-like properties, and they act as a protective reservoir for ERES components to rebuild a functional secretory pathway after re-addition of amino-acids acting as a part of a survival mechanism. Taken together, we propose that the formation of these structures is a novel stress response mechanism to provide cell viability during and after nutrient stress.
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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 Socratic graph.