Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89666
Title: Lipid bilayer stress-activated IRE-1 modulates autophagy during endoplasmic reticulum stress
Authors: Koh, Jhee Hong
Wang, Lei
Beaudoin-Chabot, Caroline
Thibault, Guillaume
Keywords: Endoplasmic Reticulum (ER)
Unfolded Protein Response (UPR)
DRNTU::Science::Biological sciences
Issue Date: 2018
Source: Koh, J. H., Wang, L., Beaudoin-Chabot, C., & Thibault, G. (2018). Lipid bilayer stress-activated IRE-1 modulates autophagy during endoplasmic reticulum stress. Journal of Cell Science, 131(22), jcs217992-. doi:10.1242/jcs.217992
Series/Report no.: Journal of Cell Science
Abstract: Metabolic disorders such as nonalcoholic fatty liver disease (NAFLD) are emerging epidemics that affect the global population. One facet of these disorders is attributed to the disturbance of membrane lipid composition. Perturbation of endoplasmic reticulum (ER) homeostasis through alteration in membrane phospholipids activates the unfolded protein response (UPR) and causes dramatic transcriptional and translational changes in the cell. To restore cellular homeostasis, the three highly conserved UPR transducers ATF6, IRE1, and PERK mediate adaptive responses upon ER stress. The homeostatic UPR cascade is well characterised under conditions of proteotoxic stress, but much less so under lipid bilayer stress induced-UPR. Disrupted phosphatidylcholine (PC) synthesis in C. elegans causes lipid bilayer stress, lipid droplet accumulation and ER stress induction. Transcriptional profiling of PC-deficient worms shows a unique subset of genes regulated in a UPR-dependent manner that is independent from proteotoxic stress. Among these, we show that autophagy is modulated through the conserved IRE-1/XBP-1 axis, strongly suggesting of the importance of autophagy in maintaining cellular homeostasis during lipid bilayer induced-UPR.
URI: https://hdl.handle.net/10356/89666
http://hdl.handle.net/10220/46714
ISSN: 0021-9533
DOI: http://dx.doi.org/10.1242/jcs.217992
Rights: © 2018 The Company of Biologists Ltd. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Cell Science, The Company of Biologists Ltd. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1242/jcs.217992].
metadata.item.grantfulltext: open
metadata.item.fulltext: With Fulltext
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