Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/161980
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dc.contributor.authorYap, Wei Shengen_US
dc.contributor.authorShyu Jr., Peteren_US
dc.contributor.authorGaspar, Maria Lauraen_US
dc.contributor.authorJesch, Stephen A.en_US
dc.contributor.authorMarvalim, Charlieen_US
dc.contributor.authorPrinz, William A.en_US
dc.contributor.authorHenry, Susan A.en_US
dc.contributor.authorThibault, Guillaumeen_US
dc.date.accessioned2022-09-30T02:19:18Z-
dc.date.available2022-09-30T02:19:18Z-
dc.date.issued2020-
dc.identifier.citationYap, W. S., Shyu Jr., P., Gaspar, M. L., Jesch, S. A., Marvalim, C., Prinz, W. A., Henry, S. A. & Thibault, G. (2020). The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis. Journal of Cell Science, 133(21), jcs248526-. https://dx.doi.org/10.1242/jcs.248526en_US
dc.identifier.issn0021-9533en_US
dc.identifier.urihttps://hdl.handle.net/10356/161980-
dc.description.abstractLipid droplets (LDs) are implicated in conditions of lipid and protein dysregulation. The fat storage-inducing transmembrane (FIT; also known as FITM) family induces LD formation. Here, we establish a model system to study the role of the Saccharomyces cerevisiae FIT homologues (ScFIT), SCS3 and YFT2, in the proteostasis and stress response pathways. While LD biogenesis and basal endoplasmic reticulum (ER) stress-induced unfolded protein response (UPR) remain unaltered in ScFIT mutants, SCS3 was found to be essential for proper stress-induced UPR activation and for viability in the absence of the sole yeast UPR transducer IRE1 Owing to not having a functional UPR, cells with mutated SCS3 exhibited an accumulation of triacylglycerol within the ER along with aberrant LD morphology, suggesting that there is a UPR-dependent compensatory mechanism that acts to mitigate lack of SCS3 Additionally, SCS3 was necessary to maintain phospholipid homeostasis. Strikingly, global protein ubiquitylation and the turnover of both ER and cytoplasmic misfolded proteins is impaired in ScFITΔ cells, while a screen for interacting partners of Scs3 identifies components of the proteostatic machinery as putative targets. Together, our data support a model where ScFITs play an important role in lipid metabolism and proteostasis beyond their defined roles in LD biogenesis.This article has an associated First Person interview with the first author of the paper.en_US
dc.description.sponsorshipNanyang Technological Universityen_US
dc.description.sponsorshipNational Research Foundation (NRF)en_US
dc.language.isoenen_US
dc.relationNRF2018NRFNSFC003SB-006en_US
dc.relation.ispartofJournal of Cell Scienceen_US
dc.relation.uri10.21979/N9/I7MXVPen_US
dc.rights© 2020 The Author(s). All rights reserved. This paper was published by The Company of Biologists Ltd in Journal of Cell Science and is made available with permission of The Author(s).en_US
dc.subjectScience::Medicineen_US
dc.titleThe yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasisen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.organizationInstitute of Molecular and Cell Biology, A*STARen_US
dc.identifier.doi10.1242/jcs.248526-
dc.description.versionPublished versionen_US
dc.identifier.pmid33033181-
dc.identifier.scopus2-s2.0-85095861718-
dc.identifier.issue21en_US
dc.identifier.volume133en_US
dc.identifier.spagejcs248526en_US
dc.subject.keywordsEndoplasmic Reticulum-Associated Degradationen_US
dc.subject.keywordsLipid Dropleten_US
dc.subject.keywordsProteostasisen_US
dc.subject.keywordsPhospholipid Metabolismen_US
dc.subject.keywordsUnfolded Protein Responseen_US
dc.description.acknowledgementThis work was supported by the Nanyang Assistant Professorship programme from the Nanyang Technological University to G.T., the National Research Foundation, Singapore, under its NRF-NSFC joint research grant call (Synthetic Biology, NRF2018NRFNSFC003SB-006) to G.T., the Nanyang Technological University Research Scholarship to P.J.S. (predoctoral fellowship), the National Institutes of Health (NIH) grant GM-19629 to S.A.H., the Intramural Research Program of the NIH to W.A.P., The National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) to W.A.P.en_US
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