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http://purl.uniprot.org/citations/12175335http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12175335http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12175335http://www.w3.org/2000/01/rdf-schema#comment"The macropinocytic pathway in Dictyostelium discoideum is organized linearly. After actin-driven internalization, fluid material passes sequentially from endosomes to lysosomes, where molecules are degraded and absorbed. Residual material is exocytosed via post-lysosomal compartments. Syntaxin 7 is a SNARE (soluble N -ethylmaleimide-sensitive fusion protein attachment protein receptor) protein that is present and active in D. discoideum endosomes [Bogdanovic, Bruckert, Morio and Satre (2000) J. Biol. Chem. 275, 36691-36697]. Here we report the identification of its main SNARE partners by co-immunoprecipitation and MS peptide sequencing. The syntaxin 7 complex contains two co-t-SNAREs [Vti1 (Vps10p tail interactor 1) and syntaxin 8] and a v-SNARE [VAMP7 (vesicle-associated membrane protein 7)] (where t-SNAREs are SNAREs of the target compartment and v-SNAREs are SNAREs present in donor vesicles). In endosomes and in vitro, syntaxin 7, Vti1 and syntaxin 8 form a complex that is able to bind VAMP7. Antibodies to syntaxin 8 and a soluble recombinant VAMP7 fragment both inhibit in vitro reconstituted D. discoideum endosome fusion. The lysosomal content of syntaxin 7, Vti1, syntaxin 8 and VAMP7 is low compared with that in endosomes, implying a highly active recycling or retention mechanism. A likely model is that VAMP7 is a v-SNARE present on vesicles carrying lysosomal enzymes, and that the syntaxin 7-Vti1-syntaxin 8 t-SNARE complex is associated with incoming endocytic material."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.org/dc/terms/identifier"doi:10.1042/bj20020845"xsd:string
http://purl.uniprot.org/citations/12175335http://purl.org/dc/terms/identifier"doi:10.1042/bj20020845"xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Garin J."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Garin J."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Morio T."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Morio T."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Satre M."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Satre M."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Bennett N."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Bennett N."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Bogdanovic A."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Bogdanovic A."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Bruckert F."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Bruckert F."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Louwagie M."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Louwagie M."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Kieffer S."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/author"Kieffer S."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/12175335http://purl.uniprot.org/core/name"Biochem. J."xsd:string