In this section
@article{Adams:2019:10.3389/fmolb.2019.00011,
author = {Adams, CJ and Kopp, MC and Larburu, N and Nowak, PR and Ali, MMU},
doi = {10.3389/fmolb.2019.00011},
journal = {Frontiers in Molecular Biosciences},
title = {Structure and molecular mechanism of ER stress signaling by the unfolded protein response signal activator IRE1},
url = {http://dx.doi.org/10.3389/fmolb.2019.00011},
volume = {6},
year = {2019}
}
TY - JOUR
AB - 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.
AU - Adams,CJ
AU - Kopp,MC
AU - Larburu,N
AU - Nowak,PR
AU - Ali,MMU
DO - 10.3389/fmolb.2019.00011
PY - 2019///
SN - 2296-889X
TI - Structure and molecular mechanism of ER stress signaling by the unfolded protein response signal activator IRE1
T2 - Frontiers in Molecular Biosciences
UR - http://dx.doi.org/10.3389/fmolb.2019.00011
VL - 6
ER -
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