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http://purl.uniprot.org/citations/26900751http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26900751http://www.w3.org/2000/01/rdf-schema#comment"Receptor-interacting protein kinase 3 (RIPK3) functions as a key regulator of necroptosis. Here, we report that the RIPK3 expression level is negatively regulated by CHIP (carboxyl terminus of Hsp70-interacting protein; also known as STUB1) E3 ligase-mediated ubiquitylation. Chip(-/-) mouse embryonic fibroblasts and CHIP-depleted L929 and HT-29 cells exhibited higher levels of RIPK3 expression, resulting in increased sensitivity to necroptosis induced by TNF (also known as TNFα). These phenomena are due to the CHIP-mediated ubiquitylation of RIPK3, which leads to its lysosomal degradation. Interestingly, RIPK1 expression is also negatively regulated by CHIP-mediated ubiquitylation, validating the major role of CHIP in necrosome formation and sensitivity to TNF-mediated necroptosis. Chip(-/-) mice (C57BL/6) exhibit inflammation in the thymus and massive cell death and disintegration in the small intestinal tract, and die within a few weeks after birth. These phenotypes are rescued by crossing with Ripk3(-/-) mice. These results imply that CHIP is a bona fide negative regulator of the RIPK1-RIPK3 necrosome formation leading to desensitization of TNF-mediated necroptosis."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.org/dc/terms/identifier"doi:10.1038/ncb3314"xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Kim J.H."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Lee H.K."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Lee C."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Shin J."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Song J."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Seo J."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Han S.Y."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Vandenabeele P."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Jeong M."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Seong J.K."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Lee E.W."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Dondelinger Y."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Seong D."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/author"Sung H."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/pages"291-302"xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/title"CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3."xsd:string
http://purl.uniprot.org/citations/26900751http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/26900751http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26900751
http://purl.uniprot.org/citations/26900751http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26900751
http://purl.uniprot.org/uniprot/#_E9PZP3-mappedCitation-26900751http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26900751