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10.15252/embj.201694300 http://scihub22266oqcxt.onion/10.15252/embj.201694300 C5007551!5007551 !27307491     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27307491 &cmd=llinks): Failed to open stream: HTTP request failed! 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SPATA2 links CYLD to the TNF-? receptor signaling complex and modulates the receptor signaling outcomes |pdf=|usr=}}{{27307491 }} gab.com Text SPATA2 links CYLD to the TNF- receptor signaling complex and modulates the receptor signaling outcomes JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=27307491 #FOAvip TNF-? is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-? 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-? stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-? 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-?B and inhibits TNF-?-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-? signaling. Taken together, our study draws a detailed map of TNF-? signaling, identifies SPATA2 as a novel component of TNF-? signaling, and provides a rich resource for further functional investigations. Twit Text FOAVip SPATA2 links CYLD to the TNF- receptor signaling complex and modulates the receptor signaling outcomes ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=27307491 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27307491 #FOAvip English Wikipedia <ref>{{Cite pmid|27307491 }}</ref> SPATA2 links CYLD to the TNF-? receptor signaling complex and modulates the receptor signaling outcomes #MMPMID27307491 Wagner SA ; Satpathy S ; Beli P ; Choudhary C EMBO J 2016[Sep]; 35 (17 ): 1868-84 PMID27307491 show ga TNF-? is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-? 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-? stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-? 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-?B and inhibits TNF-?-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-? signaling. Taken together, our study draws a detailed map of TNF-? signaling, identifies SPATA2 as a novel component of TNF-? signaling, and provides a rich resource for further functional investigations. |*Signal Transduction [MESH] |Cell Line [MESH] |Deubiquitinating Enzyme CYLD [MESH] |Humans [MESH] |Mass Spectrometry [MESH] |Phosphorylation [MESH] |Protein Interaction Mapping [MESH] |Protein Processing, Post-Translational [MESH] |Proteins/*metabolism [MESH] |Proteome/analysis [MESH] |Receptors, Tumor Necrosis Factor/*metabolism [MESH] |Tumor Necrosis Factor-alpha/*metabolism [MESH] |Tumor Suppressor Proteins/*metabolism [MESH] |Ubiquitin-Protein Ligases/metabolism [MESH]SPATA2 links CYLD to the TNF-? receptor signaling complex and modulate(epmc).pdf DeepDyve Pubget Overpricing