{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mizuike A"],"funding":["Japan Society for the Promotion of Science"],"pagination":["e0215009"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6453485"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(4)"],"pubmed_abstract":["Interorganelle phospholipid transfer is critical for eukaryotic membrane biogenesis. In the yeast Saccharomyces cerevisiae, phosphatidylserine (PS) synthesized by PS synthase, Pss1, in the endoplasmic reticulum (ER) is decarboxylated to phosphatidylethanolamine (PE) by PS decarboxylase, Psd1, in the ER and mitochondria or by Psd2 in the endosome, Golgi, and/or vacuole, but the mechanism of interorganelle PS transport remains to be elucidated. Here we report that Sfh1, a member of Sec14 family proteins of S. cerevisiae, possesses the ability to enhance PE production by Psd2. Overexpression of SFH1 in the strain defective in Psd1 restored its growth on non-fermentable carbon sources and increased the intracellular and mitochondrial PE levels. Sfh1 was found to bind various phospholipids, inc"],"journal":["PloS one"],"pubmed_title":["Suppression of respiratory growth defect of mitochondrial phosphatidylserine decarboxylase deficient mutant by overproduction of Sfh1, a Sec14 homolog, in yeast."],"pmcid":["PMC6453485"],"funding_grant_id":["17K07710","20•6296","15J10871"],"pubmed_authors":["Mizuike A","Kobayashi S","Rikukawa T","Horiuchi H","Ohta A","Fukuda R"],"additional_accession":[]},"is_claimable":false,"name":"Suppression of respiratory growth defect of mitochondrial phosphatidylserine decarboxylase deficient mutant by overproduction of Sfh1, a Sec14 homolog, in yeast.","description":"Interorganelle phospholipid transfer is critical for eukaryotic membrane biogenesis. In the yeast Saccharomyces cerevisiae, phosphatidylserine (PS) synthesized by PS synthase, Pss1, in the endoplasmic reticulum (ER) is decarboxylated to phosphatidylethanolamine (PE) by PS decarboxylase, Psd1, in the ER and mitochondria or by Psd2 in the endosome, Golgi, and/or vacuole, but the mechanism of interorganelle PS transport remains to be elucidated. Here we report that Sfh1, a member of Sec14 family proteins of S. cerevisiae, possesses the ability to enhance PE production by Psd2. Overexpression of SFH1 in the strain defective in Psd1 restored its growth on non-fermentable carbon sources and increased the intracellular and mitochondrial PE levels. Sfh1 was found to bind various phospholipids, inc","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2025-04-04T13:25:30.489Z","creation":"2019-06-06T21:09:07Z"},"accession":"S-EPMC6453485","cross_references":{"pubmed":["30958856"],"doi":["10.1371/journal.pone.0215009"]}}