ArticleScientific reports2021
The ADP-binding kinase region of Ire1 directly contributes to its responsiveness to endoplasmic reticulum stress.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2024Review
- IL-33/ST2L signaling alleviates diabetic nephropathy by regulating endoplasmic reticulum stress and apoptosis.BMC nephrology · 2023Article
- Fundamental and Applicative Aspects of the Unfolded Protein Response in Yeasts.Journal of fungi (Basel, Switzerland) · 2023Review
- Endoplasmic stress sensor Ire1 is involved in cytosolic/nuclear protein quality control inFrontiers in microbiology · 2023Article
- Fast-Growing Saccharomyces cerevisiae Cells with a Constitutive Unfolded Protein Response and Their Potential for Lipidic Molecule Production.Applied and environmental microbiology · 2022Article
- Multiple Ways for Stress Sensing and Regulation of the Endoplasmic Reticulum-stress Sensors.Cell structure and function · 2021Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon endoplasmic-reticulum (ER) stress, the ER-located transmembrane protein, Ire1, is autophosphorylated and acts as an endoribonuclease to trigger the unfolded protein response (UPR). Previous biochemical studies have shown that Ire1 exhibits strong endoribonuclease activity when its cytosolic kinase region captures ADP. Here, we asked how this event contributes to the regulation of Ire1 activity. At the beginning of this study, we obtained a luminal-domain mutant of Saccharomyces cerevisiae Ire1, deltaIdeltaIIIdeltaV/Y225H Ire1, which is deduced to be controlled by none of the luminal-side regulatory events. ER-stress responsiveness of deltaIdeltaIIIdeltaV/Y225H Ire1 was largely compromised by a further mutation on the kinase region, D797N/K799N, which allows Ire1 to be activated without capturing ADP. Therefore, in addition to the ER-luminal domain of Ire1, which monitors ER conditions, the kinase region is directly involved in the ER-stress responsiveness of Ire1. We propose that potent ER stress harms cells' "vividness", increasing the cytosolic ADP/ATP ratio, and eventually strongly activates Ire1. This mechanism seems to contribute to the suppression of inappropriately potent UPR under weak ER-stress conditions.
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