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http://purl.uniprot.org/citations/26838333http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26838333http://www.w3.org/2000/01/rdf-schema#comment"Homotypic fusion of the endoplasmic reticulum (ER) is required for generating and maintaining the characteristic reticular ER membrane structures. This organelle membrane fusion process depends on the ER-bound dynamin-related GTPases, such as atlastins in animals and Sey1p in yeast. Here, to investigate whether specific lipid molecules facilitate GTPase-dependent ER membrane fusion directly, we comprehensively evaluated membrane docking and lipid mixing of reconstituted proteoliposomes bearing purified Sey1p and a set of ER-mimicking lipids, including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidic acid, and ergosterol. Remarkably, we revealed that each specific lipid species contributed little to membrane docking mediated by Sey1p. Nevertheless, Sey1p-dependent lipid mixing was strongly reduced by omitting three major acidic lipids from the ER-mimicking set and, moreover, was entirely abolished by omitting either phosphatidylethanolamine or ergosterol. Our reconstitution studies thus established that physiological lipid composition is vital for lipid bilayer rearrangements in GTPase-mediated homotypic ER membrane fusion."xsd:string
http://purl.uniprot.org/citations/26838333http://purl.org/dc/terms/identifier"doi:10.1038/srep20407"xsd:string
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/author"Sugiura S."xsd:string
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/author"Mima J."xsd:string
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/pages"20407"xsd:string
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/title"Physiological lipid composition is vital for homotypic ER membrane fusion mediated by the dynamin-related GTPase Sey1p."xsd:string
http://purl.uniprot.org/citations/26838333http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/26838333http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26838333
http://purl.uniprot.org/citations/26838333http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26838333
http://purl.uniprot.org/uniprot/#_Q99287-mappedCitation-26838333http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26838333
http://purl.uniprot.org/uniprot/Q99287http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/26838333