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http://purl.uniprot.org/citations/25987606http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25987606http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25987606http://www.w3.org/2000/01/rdf-schema#comment"Organelle contact sites perform fundamental functions in cells, including lipid and ion homeostasis, membrane dynamics, and signaling. Using a forward proteomics approach in yeast, we identified new ER-mitochondria and ER-vacuole contacts specified by an uncharacterized protein, Ylr072w. Ylr072w is a conserved protein with GRAM and VASt domains that selectively transports sterols and is thus termed Ltc1, for Lipid transfer at contact site 1. Ltc1 localized to ER-mitochondria and ER-vacuole contacts via the mitochondrial import receptors Tom70/71 and the vacuolar protein Vac8, respectively. At mitochondria, Ltc1 was required for cell viability in the absence of Mdm34, a subunit of the ER-mitochondria encounter structure. At vacuoles, Ltc1 was required for sterol-enriched membrane domain formation in response to stress. Increasing the proportion of Ltc1 at vacuoles was sufficient to induce sterol-enriched vacuolar domains without stress. Thus, our data support a model in which Ltc1 is a sterol-dependent regulator of organelle and cellular homeostasis via its dual localization to ER-mitochondria and ER-vacuole contact sites."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201502033"xsd:string
http://purl.uniprot.org/citations/25987606http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201502033"xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Yamada J."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Yamada J."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Nunnari J."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Nunnari J."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Prinz W.A."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Prinz W.A."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Toulmay A."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Toulmay A."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Murley A."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Murley A."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Sarsam R.D."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/author"Sarsam R.D."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/pages"539-548"xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/pages"539-548"xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/title"Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts."xsd:string
http://purl.uniprot.org/citations/25987606http://purl.uniprot.org/core/title"Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts."xsd:string