ArticlePlant physiology2001
Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum-located transmembrane protein kinases.
Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed.
- A Bioluminescent Reporter System for Real-Time Monitoring of the Unfolded Protein Response in Plants.Plant biotechnology journal · 2026Article
- CDS-localized mNature plants · 2026Article
- Transcriptome analysis coupled with virus induced gene silencing delineates the unfolded protein response of tomato.Molecular genetics and genomics : MGG · 2026Article
- Article
- 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
- Inositol-requiring enzyme 1 alpha is essential for dentinogenesis.Frontiers in physiology · 2025Article
- Comparative analysis of IRE1s in plants: insights into heat stress adaptation in Triticum aestivum.BMC plant biology · 2024Article
- Programmed cell death regulator BAP2 is required for IRE1-mediated unfolded protein response in Arabidopsis.Nature communications · 2024Article
- Dynamics of ER stress-induced gene regulation in plants.Nature reviews. Genetics · 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
- Post-translational modifications: emerging directors of cell-fate decisions during endoplasmic reticulum stress in Arabidopsis thaliana.Biochemical Society transactions · 2024Review
- Organelle Communication with the Nucleus.Results and problems in cell differentiation · 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
- An IRE1-proteasome system signalling cohort controls cell fate determination in unresolved proteotoxic stress of the plant endoplasmic reticulum.Nature plants · 2023Article
- CRISPR-Cas-mediated unfolded protein response control for enhancing plant stress resistance.Frontiers in plant science · 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
- Relevance of the Exocyst in ArabidopsisInternational journal of molecular sciences · 2022Article
- ER Stress and the Unfolded Protein Response: Homeostatic Regulation Coordinate Plant Survival and Growth.Plants (Basel, Switzerland) · 2022Review
- Genome-Wide Prediction and Analysis ofInternational journal of molecular sciences · 2022Article
51 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A major response of eukaryotic cells to the presence of unfolded proteins in the lumen of the endoplasmic reticulum (ER) is to activate genes that encode ER-located molecular chaperones, such as the binding protein. This response, called the unfolded protein response, requires the transduction of a signal from the ER to the nucleus. In yeast (Saccharomyces cerevisiae) and mammalian cells, an ER-located transmembrane receptor protein kinase/ribonuclease called Ire1, with a sensor domain in the lumen of the ER, is the first component of this pathway. Here, we report the cloning and derived amino acid sequences of AtIre1-1 and AtIre1-2, two Arabidopsis homologs of Ire1. The two proteins are located in the perinuclear ER (based on heterologous expression of fusions with green fluorescent protein). The expression patterns of the two genes (using beta-glucuronidase fusions) are nearly nonoverlapping. We also demonstrate functional complementation of the sensor domains of the two proteins in yeast and show that the Ire1-2 protein is capable of autotransphosphorylation. These and other findings are discussed in relation to the involvement of these genes in unfolded protein response signaling in plants.
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Identifiers
11706177PMC129266What OpenQuestion holds
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.