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. 2023 Apr 21;38(3):419–428. doi: 10.1016/j.virs.2023.04.005

Fig. 6.

Fig. 6

The RING domain is necessary for TRAF7 functions. A A schematic diagram of wild-type and truncated human TRAF7 mutants. B TRAF7 interacts with TBK1 through its RING domain and WD40 repeat domain. HEK 293 ​cells (2 ​× ​105) were transfected with TBK1 and TRAF7 deletion mutants for 24 ​h and treated with MG132 before Co-IP and immunoblotting analysis. C TRAF7 relies on the RING domain to repress the activation of reporter genes. HEK 293 ​cells (2 ​× ​105) were transfected with the indicated plasmids, and after 12 ​h, cells were treated or untreated with SeV (MOI ​= ​1) for 12 ​h before luciferase analysis. D The conserved cysteine residues at position 131 of TRAF7 are necessary for TRAF7's RING domain functions. HEK 293 ​cells (2 ​× ​105) were transfected with the indicated plasmids, and after 12 ​h, cells were treated or untreated with SeV (MOI ​= ​1) for 12 ​h before luciferase analysis. E and F The conserved cysteine residues at position 131 of TRAF7 are necessary for its E3 ligase activity. HEK 293 ​cells (2 ​× ​105) were transfected with the indicated plasmids; after 12 ​h, the cells were infected or uninfected with SeV (MOI ​= ​1) for 10 ​h before Co-IP and immunoblotting analysis. (∗P ​< ​0.05; ∗∗P ​< ​0.01; ns, no significant difference).