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.
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Ubiquitination of Inositol-requiring Enzyme 1 (IRE1) by the E3 Ligase CHIP Mediates the IRE1/TRAF2/JNK Pathway [PDF]
Journal of Biological Chemistry, 2014 Deciphering the inositol-requiring enzyme 1 (IRE1) signaling pathway is fundamentally important for understanding the unfolded protein response (UPR). The ubiquitination of proteins residing on the endoplasmic reticulum (ER) membrane has been reported to be involved in the UPR, although the mechanism has yet to be fully elucidated.
Xu, Zhu +10 more
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IRE1‐mediated miRNA maturation in macrophage phosphoinositide signaling [PDF]
EMBO reports, 2020 Endoplasmic reticulum (ER) stress signaling has long been associated with various pathological states in particular with the development of diseases with an underlying inflammation, such as diabetes, liver or cardiovascular dysfunctions, and cancer. ER stress signaling is mediated by three stress sensors.
Tony Avril, Eric Chevet
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OVEREXPRESSION OF DOMINANT-NEGATIVE IRE1 ENZYME IN H1299-shE6AP CELLS INCREASES HEAT SHOCK ELEMENT-DEPENDENT TRANSCRIPTION [PDF]
Biotechnologia Acta, 2015 To investigate IRE1-dependent branch of endoplasmic reticulum stress pathway in various cancer cells we created cDNA-constructs for expression of dominant-negative inositol-requiring enzyme – 1 IRE1 and cytosolic domain of IRE1 fused on a C-terminus with
D. O. , О. H.
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In vitro RNA Cleavage Assays to Characterize IRE1-dependent RNA Decay
Bio-Protocol, 2019 The kinase/RNase IRE1 is a key effector of the cellular response to endoplasmic reticulum stress. The RNase activity of IRE1 can be measured in cells or in the test tube.
G. Karagöz +3 more
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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 +5 more
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The IRE1 Inhibitor Kira6 Curtails The Inflammatory Trait Of Immunogenic Anticancer Treatments By Targeting Hsp60 Independent Of IRE1 [PDF]
, 2020 ABSTRACT Cellular stress evoked by immunogenic anticancer treatments engaging the unfolded protein response (UPR) can elicit inflammation with conflicting therapeutic outcomes. To define cell-autonomous mechanisms coupling the UPR to molecular mediators of inflammation, we profiled the transcriptome of cancer cells responding to ...
Rufo Nicole +15 more
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Engineering ER-stress dependent non-conventional mRNA splicing
eLife, 2018 The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins.
Weihan Li +6 more
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sMEK1 promotes crosstalk between IRE1 and Akt signalling pathways: Evidence for a novel IRE1/sMEK1/Akt complex [PDF]
, 2021 Abstract The Unfolded Protein Response (UPR) is a dynamic cellular pathway that helps maintain proteostasis during endoplasmic reticulum (ER) stress. One of the key UPR sensors is IRE1, which plays a central role in managing ER stress and interacts with other cellular pathways to regulate cell homeostasis. The Akt signalling pathway, on
Ozaira Qadri +4 more
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Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers
Life Science AllianceActivation of the stress sensor Ire1 is triggered by stress-induced conformational changes in its luminal domains that promote Ire1 oligomerization.
Sam Dawes +10 more
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