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10.1038/cdd.2017.26

http://scihub22266oqcxt.onion/10.1038/cdd.2017.26
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C5520165!5520165!28282038
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suck abstract from ncbi

pmid28282038      Cell+Death+Differ 2017 ; 24 (7): 1142-7
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  • SPATA2: more than a missing link #MMPMID28282038
  • Schlicher L; Brauns-Schubert P; Schubert F; Maurer U
  • Cell Death Differ 2017[Jul]; 24 (7): 1142-7 PMID28282038show ga
  • The assembly of the TNFR1 signalling complex (TNF-RSC) depends on K63- and M1-linked ubiquitylation, promoting the recruitment of complex constituents and the stability of the complex. Ubiquitylation is a dynamic process, controlled by E3 ubiquitin ligases as well as deubiquitinases, such as CYLD and OTULIN. A novel molecule, SPATA2, which is crucial for recruiting and activating the deubiquitinase CYLD within the TNF-RSC, has now been identified by four different studies. Loss of SPATA2 was shown to result in increased TNF-, but also NOD2-mediated proinflammatory signalling. Importantly, SPATA2 is instrumental for TNF-induced cell death, and a closer look at these findings suggests that SPATA2 possibly has functions beyond promoting the activity of CYLD.
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