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Structure and molecular mechanism of ER stress signaling by the unfolded protein response signal activator IRE1

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Title: Structure and molecular mechanism of ER stress signaling by the unfolded protein response signal activator IRE1
Authors: Adams, CJ
Kopp, MC
Larburu, N
Nowak, PR
Ali, MMU
Item Type: Journal Article
Abstract: The endoplasmic reticulum (ER) is an important site for protein folding and maturation in eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its folding capacity. However, the physiological demands or aberrations in folding may result in an imbalance which can lead to the accumulation of misfolded protein, also known as “ER stress.” The unfolded protein response (UPR) is a cell-signaling system that readjusts ER folding capacity to restore protein homeostasis. The key UPR signal activator, IRE1, responds to stress by propagating the UPR signal from the ER to the cytosol. Here, we discuss the structural and molecular basis of IRE1 stress signaling, with particular focus on novel mechanistic advances. We draw a comparison between the recently proposed allosteric model for UPR induction and the role of Hsp70 during polypeptide import to the mitochondrial matrix.
Issue Date: 12-Mar-2019
Date of Acceptance: 15-Feb-2019
URI: http://hdl.handle.net/10044/1/67623
DOI: https://dx.doi.org/10.3389/fmolb.2019.00011
ISSN: 2296-889X
Publisher: Frontiers Media
Journal / Book Title: Frontiers in Molecular Biosciences
Volume: 6
Copyright Statement: © 2019 Adams, Kopp, Larburu, Nowak and Ali. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY, https://creativecommons.org/licenses/by/4.0/). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Sponsor/Funder: Cancer Research UK
Cancer Research UK
Funder's Grant Number: C33269/A20752
C33269/A23215
Publication Status: Published
Article Number: 11
Appears in Collections:Faculty of Natural Sciences