Results 31 to 40 of about 15,652 (205)

BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response.

PLoS Biology, 2010
The unfolded protein response (UPR) is an intracellular signaling pathway that counteracts variable stresses that impair protein folding in the endoplasmic reticulum (ER). As such, the UPR is thought to be a homeostat that finely tunes ER protein folding
David Pincus, Michael W Chevalier, Tomás Aragón, Eelco van Anken, Simon E Vidal, Hana El-Samad, Peter Walter   +6 more
doaj   +1 more source

IRE1 signaling exacerbates Alzheimer’s disease pathogenesis

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   +3 more sources

Specificity in endoplasmic reticulum-stress signaling in yeast entails a step-wise engagement of HAC1 mRNA to clusters of the stress sensor Ire1

eLife, 2014
Insufficient protein-folding capacity in the endoplasmic reticulum (ER) induces the unfolded protein response (UPR). In the ER lumen, accumulation of unfolded proteins activates the transmembrane ER-stress sensor Ire1 and drives its oligomerization.
Eelco van Anken, David Pincus, Scott Coyle, Tomás Aragón, Christof Osman, Federica Lari, Silvia Gómez Puerta, Alexei V Korennykh, Peter Walter   +8 more
doaj   +1 more source

How Ire1 senses stress [PDF]

The Journal of Cell Biology, 2007
When demands on the protein folding machinery get too great, how does the cell know? Using a series of yeast mutants, [Kimata et al.][1] now suggest that oligomerization allows an ER stress sensor protein to recognize unfolded protein and signal distress.
openaire   +1 more source

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

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   +1 more source

Tumour–host interactions in Drosophila: mechanisms in the tumour micro‐ and macroenvironment

Molecular Oncology, EarlyView.
This review examines how tumour–host crosstalk takes place at multiple levels of biological organisation, from local cell competition and immune crosstalk to organism‐wide metabolic and physiological collapse. Here, we integrate findings from Drosophila melanogaster studies that reveal conserved mechanisms through which tumours hijack host systems to ...
José Teles‐Reis, Tor Erik Rusten
wiley   +1 more source

Effects of Ire1 gene on virulence and pathogenicity of Candida albicans

Open Life Sciences
With the extensive utilization of antifungal drugs, the drug resistance of Candida albicans is progressively intensifying, and the effect of empirical treatment for C. albicans infection is not evident.
Zhao Huihai, Qin Lixia, Li Mengyan, Jiang Mengyu, Cui Mengge, Wang Hua, Hou Baohua, Wang Fukun, Jia Keran   +8 more
doaj   +1 more source

Possible Involvement of X-Box Binding Protein-1 in the Onset of Pulpitis

European Endodontic Journal
Objective: Endoplasmic reticulum (ER) stress plays important roles not only in stress avoidance, but also in cell differentiation and maturation, cell proliferation, and promotion of bone formation.
Tomoya Naruse, Katsuhiro Takeda, Kazuma Yoshida, Shinya Sasaki, Tomoki Kumagai, Yohei Takahashi, Reina Kawai, Jun Nakanishi, Hideki Shiba   +8 more
doaj   +1 more source

Pumilio protects Xbp1 mRNA from regulated Ire1-dependent decay

Nature Communications, 2022
In Drosophila, ER-targeted mRNAs are degraded by Ire1-dependent pathway. Here the authors report that the fly mRNA binding protein Pumilio is phosphorylated by Ire1 and binds to Xbp1 mRNA, protecting it from the non-canonical endoribonuclease activity of
Fátima Cairrão, Cristiana C. Santos, Adrien Le Thomas, Scot Marsters, Avi Ashkenazi, Pedro M. Domingos   +5 more
doaj   +1 more source

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   +2 more sources