Fig. 6: Als3 promotes the oligomerization of catalytically inactive caspase-8 and FADD by interacting with their DED(s). | Nature Communications

Fig. 6: Als3 promotes the oligomerization of catalytically inactive caspase-8 and FADD by interacting with their DED(s).

From: Fungal Als proteins hijack host death effector domains to promote inflammasome signaling

Fig. 6: Als3 promotes the oligomerization of catalytically inactive caspase-8 and FADD by interacting with their DED(s).The alternative text for this image may have been generated using AI.

a, b Western blot analysis of Casp8-/- 293 T cells transfected with EGFP or EGFP-N-Als3/variants and FLAG-caspase-8C360A or tagBFP-FLAG-FADD. c Immunoprecipitation and Western blot analysis of Casp8-/- 293 T lysates overexpressing either empty vector (−), FLAG-tagged human caspase-8C360A, caspase-8C360AF122E, or caspase-8C360AF122EK148DR149E with EGFP or EGFP-N-Als3. d Confocal fluorescence images of Casp8-/- 293 T cells overexpressing human caspase-8C360A and EGFP-N-Als3. The blue staining was from DAPI. Scale bar, 10 µm. e, f Immunoprecipitation and Western blot analysis of Casp8-/- 293 T lysates overexpressing either empty vector (−), tagBFP-FLAG-tagged human FADD, FADDF25R, or FADDL28E with EGFP-N-Als3. The insoluble fraction of (e) was dissolved in a buffer with urea as in all other insoluble fraction analyses, which was not applied for immunoprecipitation in (f). g Confocal immunofluorescence images of Casp8-/- 293 T cells overexpressing human FADD and EGFP-N-Als3. Scale bar, 5 µm. All results are representative of at least three individual experiments. At least 18 randomly fields were checked for the results in (d, g).

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