Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89666
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dc.contributor.authorKoh, Jhee Hongen
dc.contributor.authorWang, Leien
dc.contributor.authorBeaudoin-Chabot, Carolineen
dc.contributor.authorThibault, Guillaumeen
dc.date.accessioned2018-11-27T01:43:17Zen
dc.date.accessioned2019-12-06T17:30:43Z-
dc.date.available2018-11-27T01:43:17Zen
dc.date.available2019-12-06T17:30:43Z-
dc.date.copyright2018en
dc.date.issued2018en
dc.identifier.citationKoh, 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.217992en
dc.identifier.issn0021-9533en
dc.identifier.urihttps://hdl.handle.net/10356/89666-
dc.identifier.urihttp://hdl.handle.net/10220/46714en
dc.description.abstractMetabolic 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.en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.format.extent36 p.en
dc.language.isoenen
dc.relation.ispartofseriesJournal of Cell Scienceen
dc.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].en
dc.subjectEndoplasmic Reticulum (ER)en
dc.subjectUnfolded Protein Response (UPR)en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleLipid bilayer stress-activated IRE-1 modulates autophagy during endoplasmic reticulum stressen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1242/jcs.217992en
dc.description.versionAccepted versionen
dc.identifier.rims208998en
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