Fig. 5: Recognition of PARsylation requires the C-terminal RNF166. | Cell Death & Disease

Fig. 5: Recognition of PARsylation requires the C-terminal RNF166.

From: RNF166 promotes colorectal cancer progression by recognizing and destabilizing poly-ADP-ribosylated angiomotins

Fig. 5

A Schematic representation of WT and deletion mutants of RNF166. B, C The Di19-ZF domain is important for RNF166 to interact with Motins. D AMOT only binds to WT RNF166 and C-terminal RNF166, instead of other truncated RNF166. E Only AMOT, but not XAV939 pretreated AMOT or AMOT D/E4A could be pulled down by GST-PBD. GST-fused proteins were purified from E. coli and incubated with Flag and SBP-tagged AMOT from 293 T cells. XAV939 was added to the cell and pulldown buffer in the XAV939 treatment group. F Streptavidin pulldown to analyze the PARsylation binding activity of GST-PBD. The position of GST-PBD is marked with a black triangle. Abbreviations: GST glutathione S-transferase, PBD PAR-binding domain, ZF zinc finger.

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