http://purl.uniprot.org/citations/23620051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23620051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23620051 | http://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/23620051 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1231031"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1231031"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/author | "Dorn G.W. II"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/author | "Dorn G.W. II"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/name | "Science"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/name | "Science"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/pages | "471-475"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/pages | "471-475"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/title | "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/title | "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/volume | "340"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://purl.uniprot.org/core/volume | "340"xsd:string |
http://purl.uniprot.org/citations/23620051 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23620051 |
http://purl.uniprot.org/citations/23620051 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23620051 |
http://purl.uniprot.org/citations/23620051 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23620051 |
http://purl.uniprot.org/citations/23620051 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23620051 |
http://purl.uniprot.org/uniprot/Q80U63 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/23620051 |
http://purl.uniprot.org/uniprot/O60260 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/23620051 |