ArticleJournal of cell science2022
Stress-induced phase separation of ERES components into Sec bodies precedes ER exit inhibition in mammalian cells.
Article in Journal of cell science, 2022. 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, 29 citations in OpenAlex.
- Remaking an exit: dynamic regulation of ER exit sites by post-translational modifications.Trends in cell biology · 2026Review
- Tissue-selective COPII modulator SEC16B aggravates cardiovascular disease by promoting lipid export.The EMBO journal · 2026Article
- Endoplasmic reticulum and Golgi stress signaling-mediated regulation of protein secretion.Cellular & molecular biology letters · 2026Review
- Physiological implications of phase separation in vesicle organization and trafficking.BMC biology · 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
- Membrane-anchored mobile tethers modulate condensate wetting, localization, and migration.bioRxiv : the preprint server for biology · 2025Article
- Review
- The pathways of secretory cargo export at the endoplasmic reticulum.Nature communications · 2025Review
- Possible Involvement of X-Box Binding Protein-1 in the Onset of Pulpitis.European endodontic journal · 2024Article
- 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
- Article
- TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport.Molecular biology of the cell · 2024Article
- Protein condensates in the the secretory pathway: Unraveling biophysical interactions and function.Biophysical journal · 2024Review
- ULK/Atg1: phasing in and out of autophagy.Trends in biochemical sciences · 2024Review
- Protein condensates as flexible platforms for membrane traffic.Current opinion in cell biology · 2023Review
- The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER.Cell reports · 2023Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phase separation of components of ER exit sites (ERES) into membraneless compartments, the Sec bodies, occurs in Drosophila cells upon exposure to specific cellular stressors, namely, salt stress and amino acid starvation, and their formation is linked to the early secretory pathway inhibition. Here, we show Sec bodies also form in secretory mammalian cells upon the same stress. These reversible and membraneless structures are positive for ERES components, including both Sec16A and Sec16B isoforms and COPII subunits. We find that Sec16A, but not Sec16B, is a driver for Sec body formation, and that the coalescence of ERES components into Sec bodies occurs by fusion. Finally, we show that the stress-induced coalescence of ERES components into Sec bodies precedes ER exit inhibition, leading to their progressive depletion from ERES that become non-functional. Stress relief causes an immediate dissolution of Sec bodies and the concomitant restoration of ER exit. We propose that the dynamic conversion between ERES and Sec body assembly, driven by Sec16A, regulates protein exit from the ER during stress and upon stress relief in mammalian cells, thus providing a conserved pro-survival mechanism in response to 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 OpenQuestion graph.