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http://purl.uniprot.org/citations/11897782http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11897782http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11897782http://www.w3.org/2000/01/rdf-schema#comment"Autophagy, responsible for the delivery of cytoplasmic components to the lysosome/vacuole for degradation, is the major degradative pathway in eukaryotic cells. This process requires a ubiquitin-like protein conjugation system, in which Apg12 is covalently bound to Apg5. In the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small coiled-coil protein, Apg16. The Apg12-Apg5 and Apg16 are localized in the cytosol and pre-autophagosomal structures and play an essential role in autophagosome formation. Here we show that the Apg12-Apg5 conjugate and Apg16 form a approximately 350-kDa complex in the cytosol. Because Apg16 was suggested to form a homo-oligomer, we generated an in vivo system that allowed us to control the oligomerization state of Apg16. With this system, we demonstrated that formation of the approximately 350-kDa complex and autophagic activity depended on the oligomerization state of Apg16. These results suggest that the Apg12-Apg5 conjugate and Apg16 form a multimeric complex mediated by the Apg16 homo-oligomer, and formation of the approximately 350-kDa complex is required for autophagy in yeast."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111889200"xsd:string
http://purl.uniprot.org/citations/11897782http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111889200"xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Kuma A."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Kuma A."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Mizushima N."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Mizushima N."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Ishihara N."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/author"Ishihara N."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/pages"18619-18625"xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/pages"18619-18625"xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/title"Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/title"Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast."xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11897782http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11897782http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11897782
http://purl.uniprot.org/citations/11897782http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11897782