ArticleThe EMBO journal2024
Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering.
Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Article
- Degradation of ACSL3 by influenza A virus shifts unfolded protein response from antiviral defense to viral evasion.Virologica Sinica · 2026Article
- Targeting the UPR with Small Molecules: Emerging Strategies for Immune Regulation.Molecules (Basel, Switzerland) · 2026Review
- The unfolded protein response in progeria arteries originates from non-endothelial cell types.Life science alliance · 2026Article
- QUIRKY controls seed germination via precision degradation of ABI5.Science advances · 2025Article
- Endoplasmic Reticulum Stress in Cancer.MedComm · 2025Review
- Potential ER tubular lumen sensing by intrinsically disordered regions.Journal of cell science · 2025Article
- 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
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Conserved signaling cascades monitor protein-folding homeostasis to ensure proper cellular function. One of the evolutionary conserved key players is IRE1, which maintains endoplasmic reticulum (ER) homeostasis through the unfolded protein response (UPR). Upon accumulation of misfolded proteins in the ER, IRE1 forms clusters on the ER membrane to initiate UPR signaling. What regulates IRE1 cluster formation is not fully understood. Here, we show that the ER lumenal domain (LD) of human IRE1α forms biomolecular condensates in vitro. IRE1α LD condensates were stabilized both by binding to unfolded polypeptides as well as by tethering to model membranes, suggesting their role in assembling IRE1α into signaling-competent stable clusters. Molecular dynamics simulations indicated that weak multivalent interactions drive IRE1α LD clustering. Mutagenesis experiments identified disordered regions in IRE1α LD to control its clustering in vitro and in cells. Importantly, dysregulated clustering of IRE1α mutants led to defects in IRE1α signaling. Our results revealed that disordered regions in IRE1α LD control its clustering and suggest their role as a common strategy in regulating protein assembly on membranes.
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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.