ArticleNature2009
Messenger RNA targeting to endoplasmic reticulum stress signalling sites.
Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 178 papers.
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Who cites it
178 citing papers in PubMed, 335 citations in OpenAlex.
- Article
- RNA Structure Coordinates Translation Across the Meiotic Program.bioRxiv : the preprint server for biology · 2026Article
- Intermodulation of endoplasmic reticulum stress and ferroptosis in diabetic nephropathy: molecular mechanisms and therapeutic potentials.Apoptosis : an international journal on programmed cell death · 2025Review
- Geminivirus βV1 protein activates bZIP17/28-mediated UPR signaling to facilitate viral pathogenicity but its activity is attenuated by autophagic degradation in plants.Plant communications · 2025Article
- The role of RNA structural motifs in RNA-lipid raft interaction.Scientific reports · 2025Article
- RNA exosome-driven RNA processing instructs the duration of the unfolded protein response.Nucleic acids research · 2025Article
- Impairment in global protein synthesis uncouples UPR gene induction fromFrontiers in microbiology · 2025Article
- Comparative analysis of IRE1s in plants: insights into heat stress adaptation in Triticum aestivum.BMC plant biology · 2024Article
- 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
- Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2024Review
- Phylogeny-linked occurrence of ribosome stalling on the mRNAs of Arabidopsis unfolded protein response factor bZIP60 orthologs in divergent plant species.Nucleic acids research · 2024Article
- Exploring the IRE1 interactome: From canonical signaling functions to unexpected roles.The Journal of biological chemistry · 2024Review
- Endoplasmic reticulum stress-mediated cell death in cardiovascular disease.Cell stress & chaperones · 2024Review
- Yeast Rim11 kinase responds to glutathione-induced stress by regulating the transcription of phospholipid biosynthetic genes.Molecular biology of the cell · 2024Article
- Chemical Chaperone 4-PBA Mitigates Tumor Necrosis Factor Alpha-Induced Endoplasmic Reticulum Stress in Human Airway Smooth Muscle.International journal of molecular sciences · 2023Article
- Fundamental and Applicative Aspects of the Unfolded Protein Response in Yeasts.Journal of fungi (Basel, Switzerland) · 2023Review
- The Sequential Recruitments of Rab-GTPase Ypt1p and the NNS Complex onto pre-Molecular and cellular biology · 2023Article
- Development of a GFP biosensor reporter for the unfolded protein response-signaling pathway in plants: incorporation of the bZIP60 intron into the GFP gene.Plant signaling & behavior · 2022Article
- An improved imaging system that corrects MS2-induced RNA destabilization.Nature methods · 2022Article
118 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Deficiencies in the protein-folding capacity of the endoplasmic reticulum (ER) in all eukaryotic cells lead to ER stress and trigger the unfolded protein response (UPR). ER stress is sensed by Ire1, a transmembrane kinase/endoribonuclease, which initiates the non-conventional splicing of the messenger RNA encoding a key transcription activator, Hac1 in yeast or XBP1 in metazoans. In the absence of ER stress, ribosomes are stalled on unspliced HAC1 mRNA. The translational control is imposed by a base-pairing interaction between the HAC1 intron and the HAC1 5' untranslated region. After excision of the intron, transfer RNA ligase joins the severed exons, lifting the translational block and allowing synthesis of Hac1 from the spliced HAC1 mRNA to ensue. Hac1 in turn drives the UPR gene expression program comprising 7-8% of the yeast genome to counteract ER stress. Here we show that, on activation, Ire1 molecules cluster in the ER membrane into discrete foci of higher-order oligomers, to which unspliced HAC1 mRNA is recruited by means of a conserved bipartite targeting element contained in the 3' untranslated region. Disruption of either Ire1 clustering or HAC1 mRNA recruitment impairs UPR signalling. The HAC1 3' untranslated region element is sufficient to target other mRNAs to Ire1 foci, as long as their translation is repressed. Translational repression afforded by the intron fulfils this requirement for HAC1 mRNA. Recruitment of mRNA to signalling centres provides a new paradigm for the control of eukaryotic gene expression.
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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.