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http://purl.uniprot.org/citations/29358703http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29358703http://www.w3.org/2000/01/rdf-schema#comment"Receptor-interacting protein kinase 3 (RIP3)-regulated production of reactive oxygen species (ROS) positively feeds back on tumour necrosis factor (TNF)-induced necroptosis, a type of programmed necrosis. Glutamine catabolism is known to contribute to RIP3-mediated ROS induction, but the major contributor is unknown. Here, we show that RIP3 activates the pyruvate dehydrogenase complex (PDC, also known as PDH), the rate-limiting enzyme linking glycolysis to aerobic respiration, by directly phosphorylating the PDC E3 subunit (PDC-E3) on T135. Upon activation, PDC enhances aerobic respiration and subsequent mitochondrial ROS production. Unexpectedly, mixed-lineage kinase domain-like (MLKL) is also required for the induction of aerobic respiration, and we further show that it is required for RIP3 translocation to meet mitochondria-localized PDC. Our data uncover a regulation mechanism of PDC activity, show that PDC activation by RIP3 is most likely the major mechanism activated by TNF to increase aerobic respiration and its by-product ROS, and suggest that RIP3-dependent induction of aerobic respiration contributes to pathologies related to oxidative stress."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.org/dc/terms/identifier"doi:10.1038/s41556-017-0022-y"xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Han J."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"He X."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Liang Y."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Wu J."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Zhao S."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Yang Z."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Zhou D."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Ni H."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/author"Zhong C.Q."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/pages"186-197"xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/title"RIP3 targets pyruvate dehydrogenase complex to increase aerobic respiration in TNF-induced necroptosis."xsd:string
http://purl.uniprot.org/citations/29358703http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/29358703http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29358703
http://purl.uniprot.org/citations/29358703http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/29358703
http://purl.uniprot.org/uniprot/#_E9PZP3-mappedCitation-29358703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29358703
http://purl.uniprot.org/uniprot/#_A0A2I3BPT3-mappedCitation-29358703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29358703
http://purl.uniprot.org/uniprot/#_A0A2I3BQW9-mappedCitation-29358703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29358703