Fig. 5: MAPK inhibition promotes ZNF263 degradation through the ubiquitin pathway.
From: The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma epigenetically
a Immunoblotting revealing the half-life of ZNF263 protein upon treatment with Trametinib. b The structure of full-length ZNF263 and ZNF263-ΔD (lacking the SCAN and D-domain). Experiments with IP followed by immunoblotting showing the interaction between ERK2 and ZNF263, either with ZNF263 antibody (c) or ERK2 antibody (d) for immunoprecipitation. e Representative confocal images of HEK293 cells co-transfected with ZNF263-GFP (green) and ERK2-RFP (red). The merged images show strong co-localization of ZNF263 and ERK2 in the nuclei (top). Trametinib treatment reduces the co-localization as indicated by the arrow (bottom). f IP and western blotting analysis showing p-ERK1/2 and ERK2 bind to full-length ZNF263 protein, but not ZNF263-ΔD. U251 cells were transfected with full-length ZNF263 and ZNF263-ΔD vectors, respectively. g Western blotting showing the half-life of full-length ZNF263 and ZNF263-ΔD protein with or without Trametinib treatment. *p < 0.05; **p < 0.01; ***p < 0.001.
