ArticleScience (New York, N.Y.)2021
The stress-sensing domain of activated IRE1α forms helical filaments in narrow ER membrane tubes.
Article in Science (New York, N.Y.), 2021. 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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The trial behind it
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Who cites it
20 citing papers in PubMed.
- Article
- Steric confinement-induced emission probe for monitoring protein conformations in live cells.Communications chemistry · 2026Article
- Homeostasis control in health and disease by the unfolded protein response.Nature reviews. Molecular cell biology · 2025Review
- The role of bHLH-PAS transcription factors in endoplasmic reticulum stress.Frontiers in molecular biosciences · 2025Review
- Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering.The EMBO journal · 2024Article
- Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers.Life science alliance · 2024Article
- Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2024Review
- Protein translation rate determines neocortical neuron fate.Nature communications · 2024Article
- Quantifying organellar ultrastructure in cryo-electron tomography using a surface morphometrics pipeline.The Journal of cell biology · 2023Article
- Article
- Strength in numbers: effect of protein crowding on the shape of cell membranes.Biochemical Society transactions · 2022Review
- Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.Chemical reviews · 2022Review
- Endoplasmic Reticulum in Metaplasticity: From Information Processing to Synaptic Proteostasis.Molecular neurobiology · 2022Review
- Article
- Article
- Genomic and clinical features of endoplasmic reticulum stress factor in digestive system pan-cancer studies.Frontiers in oncology · 2022Article
- Insights Into the Biogenesis and Emerging Functions of Lipid Droplets From Unbiased Molecular Profiling Approaches.Frontiers in cell and developmental biology · 2022Review
- Decoding non-canonical mRNA decay by the endoplasmic-reticulum stress sensor IRE1α.Nature communications · 2021Article
- Review
- The stress-sensing domain of activated IRE1α forms helical filaments in narrow ER membrane tubes.Science (New York, N.Y.) · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The signaling network of the unfolded protein response (UPR) adjusts the protein-folding capacity of the endoplasmic reticulum (ER) according to need. The most conserved UPR sensor, IRE1α, spans the ER membrane and activates through oligomerization. IRE1α oligomers accumulate in dynamic foci. We determined the in situ structure of IRE1α foci by cryogenic correlated light and electron microscopy combined with electron cryo-tomography and complementary immuno–electron microscopy in mammalian cell lines. IRE1α foci localized to a network of narrow anastomosing ER tubes (diameter, ~28 nm) with complex branching. The lumen of the tubes contained protein filaments, which were likely composed of arrays of IRE1α lumenal domain dimers that were arranged in two intertwined, left-handed helices. This specialized ER subdomain may play a role in modulating IRE1α signaling.
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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.