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http://purl.uniprot.org/citations/28920954http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28920954http://www.w3.org/2000/01/rdf-schema#comment"Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by phosphoproteomic screens using LPS-treated macrophages and stress-stimulated embryonic fibroblasts. p38MAPK/MK2 interact with RIPK1 in a cytoplasmic complex and MK2 phosphorylates mouse RIPK1 at Ser321/336 in response to pro-inflammatory stimuli, such as TNF and LPS, and infection with the pathogen Yersinia enterocolitica. MK2 phosphorylation inhibits RIPK1 autophosphorylation, curtails RIPK1 integration into cytoplasmic cytotoxic complexes, and suppresses RIPK1-dependent apoptosis and necroptosis. In Yersinia-infected macrophages, RIPK1 phosphorylation by MK2 protects against infection-induced apoptosis, a process targeted by Yersinia outer protein P (YopP). YopP suppresses p38MAPK/MK2 activation to increase Yersinia-driven apoptosis. Hence, MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.org/dc/terms/identifier"doi:10.1038/ncb3614"xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Fischer J."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Aepfelbacher M."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Gaestel M."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Menon M.B."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Kotlyarov A."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Gropengiesser J."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Ruckdeschel K."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Ronkina N."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Lafera J."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Novikova L."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Czymmeck N."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Deuretzbacher A."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/author"Schimmeck H."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/pages"1248-1259"xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/title"p38pisup>MAPKpi/sup>/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection."xsd:string
http://purl.uniprot.org/citations/28920954http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/28920954http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28920954
http://purl.uniprot.org/citations/28920954http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28920954
http://purl.uniprot.org/uniprot/#_A0A087WSN7-mappedCitation-28920954http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28920954
http://purl.uniprot.org/uniprot/#_D3YXL4-mappedCitation-28920954http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28920954