ReviewCell structure and function2021
Multiple Ways for Stress Sensing and Regulation of the Endoplasmic Reticulum-stress Sensors.
Review in Cell structure and function, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Generating a Cell Model to Study ER Stress in iPSC-Derived Medium Spiny Neurons from a Patient with Huntington's Disease.International journal of molecular sciences · 2025Article
- Biomarker Correlations in PTSD: IL-18, IRE1, pERK, and ATF6 via Courtauld Emotional Control Scale (CECS).International journal of molecular sciences · 2025Article
- Impairment in global protein synthesis uncouples UPR gene induction fromFrontiers in microbiology · 2025Article
- Mechanistic role of mesencephalic astrocyte-derived neurotrophic factor in myocardial ischemia/reperfusion injury.Molecular medicine (Cambridge, Mass.) · 2024Article
- Exploring the therapeutic effects of sulforaphane: an in-depth review on endoplasmic reticulum stress modulation across different disease contexts.Inflammopharmacology · 2024Review
- Morroniside Protects C2C12 Myoblasts from Oxidative Damage Caused by ROS-Mediated Mitochondrial Damage and Induction of Endoplasmic Reticulum Stress.Biomolecules & therapeutics · 2024Article
- Dual roles of UPRJournal of molecular medicine (Berlin, Germany) · 2023Review
- Endoplasmic stress sensor Ire1 is involved in cytosolic/nuclear protein quality control inFrontiers in microbiology · 2023Article
- CCDC85A is regulated by miR-224-3p and augments cancer cell resistance to endoplasmic reticulum stress.Frontiers in oncology · 2023Article
- Fast-Growing Saccharomyces cerevisiae Cells with a Constitutive Unfolded Protein Response and Their Potential for Lipidic Molecule Production.Applied and environmental microbiology · 2022Article
- Induction of the Unfolded Protein Response at High Temperature inInternational journal of molecular sciences · 2022Article
- Review
- Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1.The Journal of cell biology · 2021Article
- Induction and Aggravation of the Endoplasmic-Reticulum Stress by Membrane-Lipid Metabolic Intermediate Phosphatidyl-Frontiers in cell and developmental biology · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dysfunction of the endoplasmic reticulum (ER), so-called ER stress, is accompanied with accumulation of unfolded proteins in the ER. Eukaryotic cells commonly have an ER-located transmembrane protein, Ire1, which triggers cellular protective events against ER stress. In animal cells, PERK and ATF6 also initiate the ER-stress response. As a common strategy to control the activity of these ER-stress sensors, an ER-resident molecular chaperone, BiP, serves as their negative regulator, and dissociates from them in response to ER stress. Although it sounds reasonable that unfolded proteins and Ire1 compete for BiP association, some publications argue against this competition model. Moreover, yeast Ire1 (and possibly also the mammalian major Ire1 paralogue IRE1α) directly detects ER-accumulated unfolded proteins, and subsequently oligomerizes for its further activation. Apart from protein misfolding, the saturation of membrane phospholipids is another outcome of ER-stressing stimuli, which is sensed by the transmembrane domain of Ire1. This review describes the canonical and up-to-date insights concerning stress-sensing and regulatory mechanisms of yeast Ire1 and metazoan ER-stress sensors.Key words: endoplasmic reticulum, stress, unfolded protein response, molecular chaperone.
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