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http://purl.uniprot.org/citations/12727870http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12727870http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12727870http://www.w3.org/2000/01/rdf-schema#comment"Intracellular lipid traffic is mediated both by membrane vesicles and by a number of non-vesicular pathways facilitated by cytoplasmic lipid binding proteins. For these proteins to act effectively they must be targeted accurately to specific membranes. Here we identify a novel short conserved determinant called the FFAT motif that is shared by several seemingly unrelated lipid binding proteins and is also found in Opi1p, a transcriptional regulator of phospholipid synthesis in yeast. FFAT motifs act as membrane-targeting determinants by their direct interaction with homologues of VAMP-associated protein (VAP), a conserved endoplasmic reticulum (ER) protein. In budding yeast, all four proteins with FFAT motifs interact with Scs2p, a homologue of VAP, to target the ER to some extent. The precise intracellular distribution of each of these proteins depends on the integration of the FFAT-Scs2p interaction with other targeting determinants, and the interaction is functionally significant. We conclude that binding to a VAP homologue is a common mechanism by which proteins with FFAT motifs, most of which are involved in lipid metabolism, target ER membranes."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg201"xsd:string
http://purl.uniprot.org/citations/12727870http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg201"xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/author"Roy A."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/author"Roy A."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/author"Loewen C.J.R."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/author"Loewen C.J.R."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/author"Levine T.P."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/author"Levine T.P."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/pages"2025-2035"xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/pages"2025-2035"xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/title"A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/title"A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP."xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12727870http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12727870http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12727870
http://purl.uniprot.org/citations/12727870http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12727870
http://purl.uniprot.org/citations/12727870http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12727870
http://purl.uniprot.org/citations/12727870http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12727870