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http://purl.uniprot.org/citations/20008566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20008566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20008566http://www.w3.org/2000/01/rdf-schema#comment"Sterols are transferred between cellular membranes by vesicular and poorly understood nonvesicular pathways. Oxysterol-binding protein-related proteins (ORPs) have been implicated in sterol sensing and nonvesicular transport. In this study, we show that yeast ORPs use a novel mechanism that allows regulated sterol transfer between closely apposed membranes, such as organelle contact sites. We find that the core lipid-binding domain found in all ORPs can simultaneously bind two membranes. Using Osh4p/Kes1p as a representative ORP, we show that ORPs have at least two membrane-binding surfaces; one near the mouth of the sterol-binding pocket and a distal site that can bind a second membrane. The distal site is required for the protein to function in cells and, remarkably, regulates the rate at which Osh4p extracts and delivers sterols in a phosphoinositide-dependent manner. Together, these findings suggest a new model of how ORPs could sense and regulate the lipid composition of adjacent membranes."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200905007"xsd:string
http://purl.uniprot.org/citations/20008566http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200905007"xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Ghirlando R."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Ghirlando R."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Raychaudhuri S."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Raychaudhuri S."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Prinz W.A."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Prinz W.A."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Choi M.G."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Choi M.G."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Hinshaw J.E."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Hinshaw J.E."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Mears J.A."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Mears J.A."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Schulz T.A."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/author"Schulz T.A."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/pages"889-903"xsd:string
http://purl.uniprot.org/citations/20008566http://purl.uniprot.org/core/pages"889-903"xsd:string