ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019
Clustering of IRE1α depends on sensing ER stress but not on its RNase activity.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- The Interplay Between CaCells · 2026Review
- Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering.The EMBO journal · 2024Article
- Congress of multiple dimers is needed for cross-phosphorylation of IRE1α and its RNase activity.Life science alliance · 2024Article
- UPF3B modulates endoplasmic reticulum stress through interaction with inositol-requiring enzyme-1α.Cell death & disease · 2024Article
- Mammalian IRE1α dynamically and functionally coalesces with stress granules.Nature cell biology · 2024Article
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- Sensor dimer disruption as a new mode of action to block the IRE1-mediated unfolded protein response.Computational and structural biotechnology journal · 2022Article
- Assays to Study IRE1 Activation and Signaling.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Decoding non-canonical mRNA decay by the endoplasmic-reticulum stress sensor IRE1α.Nature communications · 2021Article
- The stress-sensing domain of activated IRE1α forms helical filaments in narrow ER membrane tubes.Science (New York, N.Y.) · 2021Article
- Dynamic regulation of mitochondrial-endoplasmic reticulum crosstalk during stem cell homeostasis and aging.Cell death & disease · 2021Review
- Multiple Ways for Stress Sensing and Regulation of the Endoplasmic Reticulum-stress Sensors.Cell structure and function · 2021Review
- The Structure, Activation and Signaling of IRE1 and Its Role in Determining Cell Fate.Biomedicines · 2021Review
- A Molecular Mechanism for Turning Off IRE1α Signaling during Endoplasmic Reticulum Stress.Cell reports · 2020Article
- New insights on human IRE1 tetramer structures based on molecular modeling.Scientific reports · 2020Article
- Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response.Open biology · 2020Review
- Dynamics and clustering of IRE1α during ER stress.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- IRE1α kinase-mediated unconventional protein secretion rescues misfolded CFTR and pendrin.Science advances · 2020Article
- Quantitative microscopy reveals dynamics and fate of clustered IRE1α.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
The sensors of the unfolded protein response react to endoplasmic reticulum (ER) stress by transient activation of their enzymatic activities, which initiate various signaling cascades. In addition, the sensor IRE1α exhibits stress-induced clustering in a transient time frame similar to activation of its endoRNase activity. Previous work had suggested that the clustering response and RNase activity of IRE1α are functionally linked, but here we show that they are independent of each other and have different behaviors and modes of activation. Although both clustering and the RNase activity are responsive to luminal stress conditions and to depletion of the ER chaperone binding protein, RNase-inactive IRE1α still clusters and, conversely, full RNase activity can be accomplished without clustering. The clusters formed by RNase-inactive IRE1α are much larger and persist longer than those induced by ER stress. Clustering requires autophosphorylation, and an IRE1α mutant whose RNase domain is responsive to ligands that bind the kinase domain forms yet a third type of stress-independent cluster, with distinct physical properties and half-lives. These data suggest that IRE1α clustering can follow distinct pathways upon activation of the sensor.-Ricci, D., Marrocco, I., Blumenthal, D., Dibos, M., Eletto, D., Vargas, J., Boyle, S., Iwamoto, Y., Chomistek, S., Paton, J. C., Paton, A. W., Argon, Y. Clustering of IRE1α depends on sensing ER stress but not on its RNase activity.
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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.