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. Author manuscript; available in PMC: 2023 Oct 9.
Published in final edited form as: Sci Signal. 2023 Mar 14;16(776):eabq0837. doi: 10.1126/scisignal.abq0837

Fig. 5. ZBP1 recruits RIPK3 to stress granules to form necrosomes.

Fig. 5.

(A) Schematic of necrosome components from previous studies (24). (B) Schematic of DSP crosslinking method used to detect necrosome formation. (C) Necrosome formation assessed after DSP crosslinking in mouse IFNα (IFN)-primed and arsenite (Ars)-treated L929 cells. *indicates an aggregated form of the protein. N=2 independent experiments. (D) Protein complex formation assessed by Western blot analysis of ZBP1 immunoprecipitates from L929 cells for RIPK3 and G3BP1. N=2 independent experiments. (E) Protein localization assessed by immunofluorescence analysis for G3BP1 and RIPK3 in L929 cells at 2 hours following arsenite treatment. N=3 sets of cells per group. Scale bar, 30 μm. (F) Protein complex formation assessed by Western blot analysis of G3BP1 immunoprecipitates from L929 and ZBP1 KO L929 cells for ZBP1 and RIPK3. N=2 independent experiments. (G) Necrosome formation assessed after DSP crosslinking in L929 and ZBP1 KO L929 cells. *indicates an aggregated form of the protein. G3BP1* blot shows bands on the same gel. N=2 independent experiments. (H) Protein localization assessed by immunofluorescence analysis for G3BP1 and RIPK3 in IFN-primed L929 and ZBP1 KO L929 cells treated with arsenite for 2 hours. N=3 sets of cells per group. Scale bar, 25 μm.