| http://purl.uniprot.org/citations/25686249 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25686249 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25686249 | http://www.w3.org/2000/01/rdf-schema#comment | "The ubiquitin-like molecule ATG12 is required for the early steps of autophagy. Recently, we identified ATG3, the E2-like enzyme required for LC3 lipidation during autophagy, as an ATG12 conjugation target. Here, we demonstrate that cells lacking ATG12-ATG3 have impaired basal autophagic flux, accumulation of perinuclear late endosomes, and impaired endolysosomal trafficking. Furthermore, we identify an interaction between ATG12-ATG3 and the ESCRT-associated protein Alix (also known as PDCD6IP) and demonstrate that ATG12-ATG3 controls multiple Alix-dependent processes including late endosome distribution, exosome biogenesis and viral budding. Similar to ATG12-ATG3, Alix is functionally required for efficient basal, but not starvation-induced, autophagy. Overall, these results identify a link between the core autophagy and ESCRT machineries and uncover a role for ATG12-ATG3 in late endosome function that is distinct from the canonical role of either ATG in autophagosome formation."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb3112"xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb3112"xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/author | "Debnath J."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/author | "Debnath J."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/author | "Malhotra R."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/author | "Malhotra R."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/author | "Murrow L."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/author | "Murrow L."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/pages | "300-310"xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/pages | "300-310"xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/title | "ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/title | "ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function."xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/volume | "17"xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://purl.uniprot.org/core/volume | "17"xsd:string |
| http://purl.uniprot.org/citations/25686249 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25686249 |
| http://purl.uniprot.org/citations/25686249 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25686249 |
| http://purl.uniprot.org/citations/25686249 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25686249 |
| http://purl.uniprot.org/citations/25686249 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25686249 |