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http://purl.uniprot.org/citations/24165940http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24165940http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24165940http://www.w3.org/2000/01/rdf-schema#comment"Autophagy is a conserved eukaryotic process of protein and organelle self-degradation within the vacuole/lysosome. Autophagy is characterized by the formation of an autophagosome, for which Vps34-dervied phosphatidylinositol 3-phosphate (PI3P) is essential. In yeast, Vps34 forms two distinct protein complexes: complex I, which functions in autophagy, and complex II, which is involved in protein sorting to the vacuole. Here we identify and characterize Atg38 as a stably associated subunit of complex I. In atg38Δ cells, autophagic activity was significantly reduced and PI3-kinase complex I dissociated into the Vps15-Vps34 and Atg14-Vps30 subcomplexes. We find that Atg38 physically interacted with Atg14 and Vps34 via its N terminus. Further biochemical analyses revealed that Atg38 homodimerizes through its C terminus and that this homodimer formation is indispensable for the integrity of complex I. These data suggest that the homodimer of Atg38 functions as a physical linkage between the Vps15-Vps34 and Atg14-Vps30 subcomplexes to facilitate complex I formation."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201304123"xsd:string
http://purl.uniprot.org/citations/24165940http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201304123"xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Arisaka F."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Arisaka F."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Hayashi Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Hayashi Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Araki Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Araki Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Ku W.C."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Ku W.C."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Ishihama Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Ishihama Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Akioka M."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"Akioka M."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"May A.I."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/author"May A.I."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/24165940http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string