title: Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae.
abstract: LDs (lipid droplets) are cellular organelles which can be found in nearly all eukaryotic cells. Despite their importance in cell biology, the mechanism underlying LD biogenesis remains largely unknown. In the present study we report that conditions of ER (endoplasmic reticulum) stress stimulate LD formation in Saccharomyces cerevisiae. We found that LDs accumulated in yeast mutants with compromised protein glycosylation or ER-associated protein degradation. Moreover, tunicamycin and Brefeldin A, agents which induce ER stress, were found to stimulate LD formation. In contrast, the restoration of protein glycosylation reduced LD accumulation. Interestingly, enhanced neutral lipids synthesis and LD formation under conditions of ER stress was not dependent on Ire1p. Lastly, we demonstrated that the absence of LDs did not compromise cell viability under ER stress. Our results suggest that although more LDs are produced, LDs are not essential to cell survival under ER stress.
authors.affiliation: School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney NSW 2052, Australia.
authors.forename: Weihua
authors.initials: W
authors.lastname: Fei
authors.forename: Han
authors.initials: H
authors.lastname: Wang
authors.forename: Xin
authors.initials: X
authors.lastname: Fu
authors.forename: Christopher
authors.initials: C
authors.lastname: Bielby
authors.forename: Hongyuan
authors.initials: H
authors.lastname: Yang
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D015153:Blotting, Western; D020126:Brefeldin A / Q000494:pharmacology; D004721:Endoplasmic Reticulum / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D050356:Lipid Metabolism / Q000187:drug effects / Q000235:genetics; D008562:Membrane Glycoproteins / Q000235:genetics / Q000502:physiology; D009154:Mutation; D015388:Organelles / Q000187:drug effects / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000502:physiology; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D002785:Sterol O-Acyltransferase / Q000378:metabolism; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D008562:Membrane Glycoproteins; D029701:Saccharomyces cerevisiae Proteins; D014415:Tunicamycin; D020126:Brefeldin A; C543386:ARE1 protein, S cerevisiae; D002785:Sterol O-Acyltransferase; C082863:IRE1 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases