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http://purl.uniprot.org/citations/8663406http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8663406http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8663406http://www.w3.org/2000/01/rdf-schema#comment"Members of the syntaxin gene family are components of protein complexes which regulate vesicle docking and/or fusion during transport of cargo through the secretory pathway of eukaryotic cells. We have previously demonstrated that syntaxin 5 is specifically required for endoplasmic reticulum to Golgi transport (Dascher, C., Matteson, J., and Balch, W. E.(1994) J. Biol. Chem. 269, 29363-29366). To extend these observations we have now cloned a protein from rat liver membranes which forms a native complex with syntaxin 5. We demonstrate that this protein is the mammalian homologue to yeast Sly1p, previously identified as a protein which genetically and biochemically interacts with the small GTPase Ypt1p and Sed5p, proteins involved in docking/fusion in the early secretory pathway of yeast. Using transient expression we find that overexpression of rat liver Sly1 (rSly1) can neutralize the dominant negative effects of excess syntaxin 5 on endoplasmic reticulum to Golgi transport. These results suggest that rSly1 functions to positively regulate syntaxin 5 function."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.27.15866"xsd:string
http://purl.uniprot.org/citations/8663406http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.27.15866"xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/author"Balch W.E."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/author"Balch W.E."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/author"Dascher C."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/author"Dascher C."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/pages"15866-15869"xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/pages"15866-15869"xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/title"Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/title"Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport."xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8663406http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8663406http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8663406
http://purl.uniprot.org/citations/8663406http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8663406
http://purl.uniprot.org/citations/8663406http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8663406
http://purl.uniprot.org/citations/8663406http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8663406
http://purl.uniprot.org/uniprot/Q62991http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8663406
http://purl.uniprot.org/uniprot/#_kb.Q62991_up.isolatedFrom_tissue.564http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8663406