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http://purl.uniprot.org/citations/23217709http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23217709http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23217709http://www.w3.org/2000/01/rdf-schema#comment"The lysosome is a degradative organelle, and its fusion with other organelles is strictly regulated. In contrast to fusion with the late endosome, the mechanisms underlying autophagosome-lysosome fusion remain unknown. Here, we identify syntaxin 17 (Stx17) as the autophagosomal SNARE required for fusion with the endosome/lysosome. Stx17 localizes to the outer membrane of completed autophagosomes but not to the isolation membrane (unclosed intermediate structures); for this reason, the lysosome does not fuse with the isolation membrane. Stx17 interacts with SNAP-29 and the endosomal/lysosomal SNARE VAMP8. Depletion of Stx17 causes accumulation of autophagosomes without degradation. Stx17 has a unique C-terminal hairpin structure mediated by two tandem transmembrane domains containing glycine zipper-like motifs, which is essential for its association with the autophagosomal membrane. These findings reveal a mechanism by which the SNARE protein is available to the completed autophagosome."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2012.11.001"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2012.11.001"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/author"Mizushima N."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/author"Mizushima N."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/author"Itakura E."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/author"Itakura E."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/author"Kishi-Itakura C."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/author"Kishi-Itakura C."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/pages"1256-1269"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/pages"1256-1269"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/title"The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/title"The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes."xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/volume"151"xsd:string
http://purl.uniprot.org/citations/23217709http://purl.uniprot.org/core/volume"151"xsd:string
http://purl.uniprot.org/citations/23217709http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23217709
http://purl.uniprot.org/citations/23217709http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23217709
http://purl.uniprot.org/citations/23217709http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23217709
http://purl.uniprot.org/citations/23217709http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23217709