Results 11 to 20 of about 19,138 (225)

Dual IRE1 targets: Determinants of the cell fate? [PDF]

The FEBS Journal, Volume 293, Issue 18, Page 5423-5432, September 2026.
IRE1 is an ER stress sensor that restores protein homeostasis through two signaling activities: XBP1s, which upregulates its target gene expression or RIDD which downregulates its target transcripts. We recently identified Dual IRE1 Targets (DIT) which are modulated by both XBP1s and RIDD activities.
Eva Billat, Léane Legrand, Tony Avril, Elodie Lafont   +3 more
wiley   +3 more sources

Mechanosensing at the endoplasmic reticulum by IRE1

Abstract Sensing and integration of mechanical forces in eukaryotic cells have largely been attributed to the plasma membrane and the nucleus. Here, we identify the endoplasmic reticulum (ER) as an autonomous mechanosensitive organelle and uncover IRE1 as an ER-resident mechanosensor.
Hesso Farhan, Michaela Mayr, Luiz Garcia-Souza, Murphy McDermott, Utku Horzum, Yannick Frey, Margot Haun, Stephan Geley, Chao Jiang, Mattias Luber, Anush Bakunts, Camilla Pirolo, Alesia Yakimchyk, Klaus Liedl, Wylie Stroberg, Timo Betz, Liam Holt   +16 more
core   +4 more sources

The IRE1‐XBP1s Axis Drives Inflammatory Osteolysis by Regulating a 5‐HT Dependent Endogenous Anti‐Autophagy Mechanism [PDF]

Advanced Science, EarlyView.
A previously unrecognized IRE1‐XBP1s‐Slc6a4 signaling axis links endoplasmic reticulum stress to serotonin metabolism, autophagy, and inflammatory osteoclastogenesis. By promoting intracellular serotonin uptake and reducing endogenous 3‐methyladenine accumulation, this pathway accelerates inflammatory bone destruction and provides a promising ...
Pengchao Yang, Binxiang Zhu, Yuzhi He, Yang Tian, Honglei Kang, Shian Hu, Pengju Wang, Yong Xu, Zhuowei Lei, Peijun Qi, Hao Yang, Yang Lin, Yimin Dong, Feng Li, Hanfeng Guan   +14 more
wiley   +2 more sources

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, Nowak, Piotr R, Carrara, Marta, Ali, Maruf MU   +3 more
openaire   +5 more sources

Structure-Based Drug Discovery of IRE1 Modulators

, 2022
IRE1α (inositol-requiring enzyme 1 alpha, referred to IRE1 hereafter) is an Endoplasmic Reticulum (ER) resident transmembrane enzyme with cytosolic kinase/RNAse activities. Upon ER stress IRE1 is activated through trans-autophosphorylation and oligomerization, resulting in a conformational change of the RNase domain, thereby promoting two signaling ...
Pelizzari Raymundo, Diana, Eriksson, Leif A, Chevet, Eric, Guillory, Xavier   +3 more
openaire   +3 more sources

Protomer alignment modulates specificity of RNA substrate recognition by Ire1 [PDF]

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, Kelly Crotty, Diego Garrido Ruiz, Mark Voorhies, Carlos Rivera, Anita Sil, R Dyche Mullins, Matthew P Jacobson, Jirka Peschek, Peter Walter   +9 more
doaj   +2 more sources

IRE1 signaling exacerbates Alzheimer’s disease pathogenesis [PDF]

Acta Neuropathologica, 2017
Altered proteostasis is a salient feature of Alzheimer's disease (AD), highlighting the occurrence of endoplasmic reticulum (ER) stress and abnormal protein aggregation. ER stress triggers the activation of the unfolded protein response (UPR), a signaling pathway that enforces adaptive programs to sustain proteostasis or eliminate terminally damaged ...
Durán Aniotz, Claudia, Cornejo, Victor Hugo, Espinoza, Sandra, Ardiles, Álvaro O., Medinas Bilches, Danilo, Salazar, Claudia, Foley, Andrew, Gajardo, Ivana, Thielen, Peter, Iwawaki, Takao, Scheper, Wiep, Soto, Claudio, Palacios, Adrian G., Hoozemans, Jeroen J.M., Hetz Flores, Claudio   +14 more
openaire   +4 more sources

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, Dimitrios Doultsinos, Raphael Pineau, Chloé Sauzay, Thodoris Koutsandreas, Timothy Langlais, Antonio Carlesso, Elena Gkotsi, Luc Negroni, Tony Avril, Aristotelis Chatziioannou, Eric Chevet, Leif A. Eriksson, Xavier Guillory   +13 more
doaj   +3 more sources

The unfolded protein sensor IRE1 is essential for homeostatic dendritic cell maturation [PDF]

Nature Communications
Conventional type I dendritic cells (cDC1s) undergo homeostatic maturation upon apoptotic cell engulfment, hallmarked by the activation of the transcription factor LXRβ, which mediates cholesterol efflux and dampens interferon-stimulated gene expression.
Victor Bosteels, Sandra Maréchal, Eva Cloots, Farzaneh Fayazpour, Clint De Nolf, Laurien Van Heddegem, Simon J. Tavernier, Sofie Rennen, Seraja Amstelveen, Liesbet Martens, Evelien Van De Velde, Delphine De Sutter, Annick Verhee, Kim Deswarte, Wouter Saelens, Louis Boon, Julie Van Duyse, Gert Van Isterdael, Isabelle Guillas, Yvan Saeys, Bruno De Geest, Sven Eyckerman, Pieter Mestdagh, Bart N. Lambrecht, Wilfried Le Goff, Sophie Janssens   +25 more
doaj   +2 more sources

Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1 [PDF]

BMC Biology, 2011
Background Ire1 is a signal transduction protein in the endoplasmic reticulum (ER) membrane that serves to adjust the protein-folding capacity of the ER according to the needs of the cell.
Stroud Robert M, Finer-Moore Janet, Korostelev Andrei A, Egea Pascal F, Korennykh Alexei V, Zhang Chao, Shokat Kevan M, Walter Peter   +7 more
doaj   +4 more sources