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http://purl.uniprot.org/citations/23620051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23620051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23620051http://www.w3.org/2000/01/rdf-schema#comment"Senescent and damaged mitochondria undergo selective mitophagic elimination through mechanisms requiring two Parkinson's disease factors, the mitochondrial kinase PINK1 (PTEN-induced putative kinase protein 1; PTEN is phosphatase and tensin homolog) and the cytosolic ubiquitin ligase Parkin. The nature of the PINK-Parkin interaction and the identity of key factors directing Parkin to damaged mitochondria are unknown. We show that the mitochondrial outer membrane guanosine triphosphatase mitofusin (Mfn) 2 mediates Parkin recruitment to damaged mitochondria. Parkin bound to Mfn2 in a PINK1-dependent manner; PINK1 phosphorylated Mfn2 and promoted its Parkin-mediated ubiqitination. Ablation of Mfn2 in mouse cardiac myocytes prevented depolarization-induced translocation of Parkin to the mitochondria and suppressed mitophagy. Accumulation of morphologically and functionally abnormal mitochondria induced respiratory dysfunction in Mfn2-deficient mouse embryonic fibroblasts and cardiomyocytes and in Parkin-deficient Drosophila heart tubes, causing dilated cardiomyopathy. Thus, Mfn2 functions as a mitochondrial receptor for Parkin and is required for quality control of cardiac mitochondria."xsd:string
http://purl.uniprot.org/citations/23620051http://purl.org/dc/terms/identifier"doi:10.1126/science.1231031"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.org/dc/terms/identifier"doi:10.1126/science.1231031"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/author"Dorn G.W. II"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/author"Dorn G.W. II"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/pages"471-475"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/pages"471-475"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/title"PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/title"PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/volume"340"xsd:string
http://purl.uniprot.org/citations/23620051http://purl.uniprot.org/core/volume"340"xsd:string
http://purl.uniprot.org/citations/23620051http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23620051
http://purl.uniprot.org/citations/23620051http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23620051
http://purl.uniprot.org/citations/23620051http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23620051
http://purl.uniprot.org/citations/23620051http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23620051
http://purl.uniprot.org/uniprot/Q80U63http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23620051
http://purl.uniprot.org/uniprot/O60260http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23620051