Results 11 to 20 of about 15,652 (205)
Scientific Reports, 2021 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).
Quynh Giang Le +5 more
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eLife, 2022 Protein folding homeostasis in the endoplasmic reticulum (ER) is regulated by a signaling network, termed the unfolded protein response (UPR). Inositol-requiring enzyme 1 (IRE1) is an ER membrane-resident kinase/RNase that mediates signal transmission in
Vladislav Belyy +4 more
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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.
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Phosphoregulation of Ire1 RNase splicing activity [PDF]
Nature Communications, 2014 AbstractIre1 is activated in response to accumulation of misfolded proteins within the endoplasmic reticulum as part of the unfolded protein response (UPR). It is a unique enzyme, possessing both kinase and RNase activity that is required for specific splicing of Xbp1 mRNA leading to UPR activation.
Prischi, Filippo +3 more
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Protomer alignment modulates specificity of RNA substrate recognition by Ire1
eLife, 2021 The unfolded protein response (UPR) maintains protein folding homeostasis in the endoplasmic reticulum (ER). In metazoan cells, the Ire1 branch of the UPR initiates two functional outputs—non-conventional mRNA splicing and selective mRNA decay (RIDD). By
Weihan Li +9 more
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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
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Physiological roles of regulated Ire1 dependent decay [PDF]
Frontiers in Genetics, 2014 Inositol-requiring enzyme 1 (Ire1) is an important transducer of the unfolded protein response (UPR) that is activated by the accumulation of misfolded proteins in the endoplamic reticulum (ER stress). Activated Ire1 mediates the splicing of an intron from the mRNA of Xbp1, causing a frame-shift during translation and introducing a new carboxyl domain ...
Dina S. Coelho, Pedro M. Domingos
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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
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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
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A novel IRE1 kinase inhibitor for adjuvant glioblastoma treatment
iScience, 2023 Summary: Inositol-requiring enzyme 1 (IRE1) is a major mediator of the unfolded protein response (UPR), which is activated upon endoplasmic reticulum (ER) stress.
Diana Pelizzari-Raymundo +13 more
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