{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["6(1)"],"submitter":["Huang LJ"],"funding":["Academia Sinica"],"pubmed_abstract":["A fluid membrane containing a mix of unsaturated and saturated lipids is essential for life. However, it is unclear how lipid saturation might affect lipid homeostasis, membrane-associated proteins, and membrane organelles. Here, we generate temperature-sensitive mutants of the sole fatty acid desaturase gene <i>OLE1</i> in the budding yeast <i>Saccharomyces cerevisiae</i> Using these mutants, we show that lipid saturation triggers the endoplasmic reticulum-associated degradation (ERAD) of squalene epoxidase Erg1, a rate-limiting enzyme in sterol biosynthesis, via the E3 ligase Doa10-Ubc7 complex. We identify the P469L mutation that abolishes the lipid saturation-induced ERAD of Erg1. Overexpressed WT or stable Erg1 mutants all mislocalize into foci in the <i>ole1</i> mutant, whereas the s"],"journal":["Life science alliance"],"pagination":["e202201612"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9652772"],"repository":["biostudies-literature"],"pubmed_title":["Lipid saturation induces degradation of squalene epoxidase for sterol homeostasis and cell survival."],"pmcid":["PMC9652772"],"pubmed_authors":["Huang LJ","Chen RH"],"additional_accession":[]},"is_claimable":false,"name":"Lipid saturation induces degradation of squalene epoxidase for sterol homeostasis and cell survival.","description":"A fluid membrane containing a mix of unsaturated and saturated lipids is essential for life. However, it is unclear how lipid saturation might affect lipid homeostasis, membrane-associated proteins, and membrane organelles. Here, we generate temperature-sensitive mutants of the sole fatty acid desaturase gene <i>OLE1</i> in the budding yeast <i>Saccharomyces cerevisiae</i> Using these mutants, we show that lipid saturation triggers the endoplasmic reticulum-associated degradation (ERAD) of squalene epoxidase Erg1, a rate-limiting enzyme in sterol biosynthesis, via the E3 ligase Doa10-Ubc7 complex. We identify the P469L mutation that abolishes the lipid saturation-induced ERAD of Erg1. Overexpressed WT or stable Erg1 mutants all mislocalize into foci in the <i>ole1</i> mutant, whereas the s","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2025-04-25T23:36:07.724Z","creation":"2025-04-06T09:24:04.824Z"},"accession":"S-EPMC9652772","cross_references":{"pubmed":["36368908"],"doi":["10.26508/lsa.202201612"]}}