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http://purl.uniprot.org/citations/19549685http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19549685http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19549685http://www.w3.org/2000/01/rdf-schema#comment"Autophagy is an important catabolic process with roles in cell survival and cell death. It sequesters cytosol and organelles within double-membrane autophagosomes that deliver their contents to lysosomes for degradation. Autophagosome biogenesis is coordinated by the autophagy-related protein 4 (Atg4) family of C54 endopeptidases (Atg4A-Atg4D). These enzymes prime and then later delipidate the autophagosome marker, Atg8. Here, we show that one family member, Atg4D, is cleaved by caspase-3 in vitro and in apoptotic cells. Atg4D is a poor priming and delipidation enzyme in vitro, but truncated DeltaN63 Atg4D displays increased activity against the Atg8 paralogue, gamma-aminobutyric acid receptor-associated protein-like 1 (GABARAP-L1). In living cells, DeltaN63 Atg4D stimulates the delipidation of GABARAP-L1, whereas siRNA silencing of the gene expressing Atg4D abrogates GABARAP-L1 autophagosome formation and sensitises cells to starvation and staurosporine-induced cell death. Interestingly, Atg4D overexpression induces apoptosis, which is preceded by the caspase-independent recruitment of Atg4D to mitochondria and is facilitated by a putative C-terminal Bcl-2 homology 3 (BH3) domain. Atg4D also acquires affinity for damaged mitochondria in cells treated with hydrogen peroxide. These data suggest that Atg4D is an autophagy regulator that links mitochondrial dysfunction with apoptosis."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.org/dc/terms/identifier"doi:10.1242/jcs.046250"xsd:string
http://purl.uniprot.org/citations/19549685http://purl.org/dc/terms/identifier"doi:10.1242/jcs.046250"xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/author"Betin V.M."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/author"Betin V.M."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/author"Lane J.D."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/author"Lane J.D."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/pages"2554-2566"xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/pages"2554-2566"xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/title"Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/title"Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis."xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/volume"122"xsd:string
http://purl.uniprot.org/citations/19549685http://purl.uniprot.org/core/volume"122"xsd:string
http://purl.uniprot.org/citations/19549685http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19549685
http://purl.uniprot.org/citations/19549685http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19549685
http://purl.uniprot.org/citations/19549685http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19549685
http://purl.uniprot.org/citations/19549685http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19549685
http://purl.uniprot.org/uniprot/Q86TL0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19549685
http://purl.uniprot.org/uniprot/Q86TL0#attribution-A9EC8E9AB012EBE37B3952DD10584709http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/19549685