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http://purl.uniprot.org/citations/33773106http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33773106http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33773106http://www.w3.org/2000/01/rdf-schema#comment"The sequestration of damaged mitochondria within double-membrane structures termed autophagosomes is a key step of PINK1/Parkin mitophagy. The ATG4 family of proteases are thought to regulate autophagosome formation exclusively by processing the ubiquitin-like ATG8 family (LC3/GABARAPs). We discover that human ATG4s promote autophagosome formation independently of their protease activity and of ATG8 family processing. ATG4 proximity networks reveal a role for ATG4s and their proximity partners, including the immune-disease protein LRBA, in ATG9A vesicle trafficking to mitochondria. Artificial intelligence-directed 3D electron microscopy of phagophores shows that ATG4s promote phagophore-ER contacts during the lipid-transfer phase of autophagosome formation. We also show that ATG8 removal during autophagosome maturation does not depend on ATG4 activity. Instead, ATG4s can disassemble ATG8-protein conjugates, revealing a role for ATG4s as deubiquitinating-like enzymes. These findings establish non-canonical roles of the ATG4 family beyond the ATG8 lipidation axis and provide an AI-driven framework for rapid 3D electron microscopy."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2021.03.001"xsd:string
http://purl.uniprot.org/citations/33773106http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2021.03.001"xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Nguyen T.N."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Nguyen T.N."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Behrends C."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Behrends C."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Lazarou M."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Lazarou M."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Khuu G."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Khuu G."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Lam W.K."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Lam W.K."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Lindblom R.S.J."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Lindblom R.S.J."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Padman B.S."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Padman B.S."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Skulsuppaisarn M."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Skulsuppaisarn M."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Uoselis L."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Uoselis L."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Watts E.M."xsd:string
http://purl.uniprot.org/citations/33773106http://purl.uniprot.org/core/author"Watts E.M."xsd:string