Divergent effects of PERK and IRE1 signaling on cell viability. [PDF]
PLoS ONE, 2009 Protein misfolding in the endoplasmic reticulum (ER) activates a set of intracellular signaling pathways, collectively termed the Unfolded Protein Response (UPR). UPR signaling promotes cell survival by reducing misfolded protein levels.
Jonathan H Lin +4 more
doaj +2 more sources
Cytomegalovirus downregulates IRE1 to repress the unfolded protein response. [PDF]
PLoS Pathogens, 2013 During viral infection, a massive demand for viral glycoproteins can overwhelm the capacity of the protein folding and quality control machinery, leading to an accumulation of unfolded proteins in the endoplasmic reticulum (ER). To restore ER homeostasis,
Sebastian Stahl +9 more
doaj +3 more sources
Ubiquitin and ubiquitin‐like modifications in the endoplasmic reticulum stress response [PDF]
The FEBS Journal, Volume 293, Issue 18, Page 5481-5513, September 2026.Endoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Tony Avril +2 more
wiley +2 more sources
A novel blood brain barrier-permeable IRE1 kinase inhibitor for adjuvant glioblastoma treatment in mice. [PDF]
, 2023 Inositol Requiring Enzyme 1 (IRE1) is a bifunctional serine/threonine kinase and endoribonuclease. It is a major mediator of the Unfolded Protein Response (UPR), which is activated upon endoplasmic reticulum (ER) stress.
Xavier, Guillory +12 more
core +2 more sources
How IRE1 Reacts to ER Stress [PDF]
Cell, 2008 The long-awaited structure of the effector portion of IRE1, the endoplasmic reticulum stress transducer, is published in this issue of Cell (Lee et al., 2008). This structure provides new insight into the mysterious coupling of kinase and endoribonuclease activities in the oldest, most-conserved branch of the unfolded protein response in eukaryotes.
Ron, David, Hubbard, Stevan R.
openaire +2 more sources
The UPR Transducer IRE1 Promotes Breast Cancer Malignancy by Degrading Tumor Suppressor microRNAs
iScience, 2020 Summary: Dysregulation of inositol-requiring enzyme 1 (IRE1), the primary transducer of Unfolded Protein Response (UPR), has been observed in tumor initiation and progression, but the underlying mechanism remains to be further elucidated.
Kezhong Zhang +7 more
doaj +1 more source
Modeling and exploring human IRE1 as a strategy to design novel inhibitors: a computational approach [PDF]
, 2019 Inositol Requiring Enzyme 1 (IRE1) is a bifunctional serine/threonine kinase and endoribonuclease that is the major mediator of the Unfolded Protein Response (UPR) during endoplasmic reticulum (ER) stress.
Carlesso, Antonio
core +1 more source
Ire1 Has Distinct Catalytic Mechanisms for XBP1/HAC1 Splicing and RIDD
Cell Reports, 2014 An evolutionarily conserved unfolded protein response (UPR) component, IRE1, cleaves XBP1/HAC1 introns in order to generate spliced mRNAs that are translated into potent transcription factors.
Arvin B. Tam +2 more
doaj +1 more source
Differential Ire1 determines loser cell fate in tumor-suppressive cell competition
Cell Reports, 2023 Summary: Tumor-suppressive cell competition (TSCC) is a conserved surveillance mechanism in which neighboring cells actively eliminate oncogenic cells.
Jiadong Zheng +5 more
doaj +1 more source
Decoding non-canonical mRNA decay by the endoplasmic-reticulum stress sensor IRE1α
Nature Communications, 2021 IRE1 helps mitigate endoplasmic-reticulum stress by cleaving specific mRNAs at a conserved sequence endomotif via regulated IRE1-dependent decay (RIDD). Here the authors discover a more promiscuous IRE1 activity dubbed RIDD lacking endomotif (RIDDLE).
Adrien Le Thomas +16 more
doaj +1 more source