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http://purl.uniprot.org/citations/27307491http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27307491http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27307491http://www.w3.org/2000/01/rdf-schema#comment"TNF-α is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-α receptor-associated signaling complexes (TNF-RSC) and the architecture of the downstream signaling networks are incompletely understood. We employed quantitative mass spectrometry to demonstrate that TNF-α stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-α stimulation also induces rapid ubiquitylation of components of the TNF-RSC Temporal analysis of the TNF-RSC composition identified SPATA2 as a novel component of the TNF-RSC The predicted PUB domain in the N-terminus of SPATA2 interacts with the USP domain of CYLD, whereas the C-terminus of SPATA2 interacts with HOIP SPATA2 is required for recruitment of CYLD to the TNF-RSC Downregulation of SPATA2 augments transcriptional activation of NF-κB and inhibits TNF-α-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-α signaling. Taken together, our study draws a detailed map of TNF-α signaling, identifies SPATA2 as a novel component of TNF-α signaling, and provides a rich resource for further functional investigations."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.org/dc/terms/identifier"doi:10.15252/embj.201694300"xsd:string
http://purl.uniprot.org/citations/27307491http://purl.org/dc/terms/identifier"doi:10.15252/embj.201694300"xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Choudhary C."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Choudhary C."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Beli P."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Beli P."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Wagner S.A."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Wagner S.A."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Satpathy S."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/author"Satpathy S."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/pages"1868-1884"xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/pages"1868-1884"xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/title"SPATA2 links CYLD to the TNF-alpha receptor signaling complex and modulates the receptor signaling outcomes."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/title"SPATA2 links CYLD to the TNF-alpha receptor signaling complex and modulates the receptor signaling outcomes."xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/27307491http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/27307491http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27307491
http://purl.uniprot.org/citations/27307491http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27307491