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Fas-associating death domain containing protein (FADD)/MORT1 serves as a signal transducer of Fas-induced apoptosis. Through its amino-terminal death effector domain (DED), FADD binds to cytosolic proteins such as TRADD, a cytosolic death domaincontaining protein that asssociates with the cytosolic portion of TNF receptor, or MACH/FLICE/caspase-8, a protease with sequence homology to ICE-CED-3 protease family, in order to transduce the death signal.
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Western blot probed with FADD mAb (1F7). Lane 1 FADD (recombinant) and cell lysates Jurkat (lane 2), Raji (lane 3), HeLa (lane 4), ZR75-1 (lane 5), A431 (lane 6), and HUC-Fm (lane 7).
S166 phosphorylation facilitates necrosome formation.a BMDMs from mice of the indicated genotypes were treated with TNF (T; 10 ng ml−1), SMAC mimetic (S (Birinapant); 1 µM) and Z-VAD-FMK (Z) for 0, 2 and 4 h. RIPK1 immunoprecipitates and total cell lysates (input) were analyzed by immunoblotting with the indicated antibodies. b BMDMs from mice of the indicated genotypes were treated with TNF (T; 10 ng ml−1), SMAC mimetic (S (Birinapant); 1 µM) and Z-VAD-FMK (Z) for 2 and 4 h. Lysates were processed under non-reducing conditions and analyzed for presence of MLKL by immunoblot. c BMDMs from mice of the indicated genotypes were treated with LPS (L; 100 ng ml−1) and Z- VAD-FMK (Z) for 13 and 15 h. Lysates were processed under non-reducing or reducing conditions and analyzed by immunoblot using the indicated antibodies. d BMDMs from mice of the indicated genotypes were treated with Poly(I:C) (P; 0.5 μg ml−1) and Z-VAD-FMK (Z) for 13 and 15 h. Lysates were processed under non-reducing or reducing conditions and analyzed by immunoblot using the indicated antibodies. a, c Representative data of three independent experiments is shown. b, d Representative data of two independent experiments is shown.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation. Nat Commun (2020)
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