ArticlePlant direct2019
AtIRE1C, an unconventional isoform of the UPR master regulator AtIRE1, is functionally associated with AtIRE1B in Arabidopsis gametogenesis.
Article in Plant direct, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.
- Cell Death Signaling From Endoplasmic Reticulum Stress: Plant-Specific and Conserved Features.Frontiers in plant science · 2022Pooled it
- Dynamic regulation of proteostasis underlies thermopriming-mediated acquired thermotolerance in Arabidopsis.Plant communications · 2026Article
- Rewiring the unfolded protein response for plant growth recovery after stress.Plant communications · 2026Review
- Mitochondrial β-carbonic anhydrase is a conserved metabolic rheostat for branched-chain amino acid catabolism and metabolic flexibility.The New phytologist · 2026Article
- The bZIP transcription factor RISBZ1 balances grain filling and ER stress response in rice grains.Plant communications · 2025Article
- Comparative analysis of IRE1s in plants: insights into heat stress adaptation in Triticum aestivum.BMC plant biology · 2024Article
- Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2024Review
- Dynamics of ER stress-induced gene regulation in plants.Nature reviews. Genetics · 2024Review
- Post-translational modifications: emerging directors of cell-fate decisions during endoplasmic reticulum stress in Arabidopsis thaliana.Biochemical Society transactions · 2024Review
- Protein disulfide isomerase-9 interacts with the lumenal region of the transmembrane endoplasmic reticulum stress sensor kinase, IRE1, to modulate the unfolded protein response inFrontiers in plant science · 2024Article
- Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023Review
- The interplay of GTP-binding protein AGB1 with ER stress sensors IRE1a and IRE1b modulates Arabidopsis unfolded protein response and bacterial immunity.Plant signaling & behavior · 2022Article
- ER Stress and the Unfolded Protein Response: Homeostatic Regulation Coordinate Plant Survival and Growth.Plants (Basel, Switzerland) · 2022Review
- IRE1-mediated cytoplasmic splicing and regulated IRE1-dependent decay of mRNA in the liverwortPlant biotechnology (Tokyo, Japan) · 2022Article
- The UPR regulator IRE1 promotes balanced organ development by restricting TOR-dependent control of cellular differentiation in Arabidopsis.The Plant journal : for cell and molecular biology · 2022Article
- Unfolded protein response in balancing plant growth and stress tolerance.Frontiers in plant science · 2022Review
- Review
- Relevance of the Unfolded Protein Response to Spaceflight-Induced Transcriptional Reprogramming inAstrobiology · 2021Article
- A QuantitativeFrontiers in plant science · 2021Article
- Quantitative Proteomic Analysis of ER Stress Response Reveals both Common and Specific Features in Two Contrasting Ecotypes ofInternational journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unfolded protein response (UPR), a highly conserved set of eukaryotic intracellular signaling cascades, controls the homeostasis of the endoplasmic reticulum (ER) in normal physiological growth and situations causing accumulation of potentially toxic levels of misfolded proteins in the ER, a condition known as ER stress. During evolution, eukaryotic lineages have acquired multiple UPR effectors, which have increased the pliability of cytoprotective responses to physiological and environmental stresses. The ER-associated protein kinase and ribonuclease IRE1 is a UPR effector that is conserved from yeast to metazoans and plants. IRE1 assumes dispensable roles in growth in yeast but it is essential in mammals and plants. The Arabidopsis genome encodes two isoforms of IRE1, IRE1A and IRE1B, whose protein functional domains are conserved across eukaryotes. Here, we describe the identification of a third Arabidopsis IRE1 isoform, IRE1C. This protein lacks the ER lumenal domain that has been implicated in sensing ER stress in the IRE1 isoforms known to date. Through functional analyses, we demonstrate that IRE1C is not essential in growth and stress responses when deleted from the genome singularly or in combination with an
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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.