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Resolution: standard / high Figure 3.
Model for Vif-induced degradation of APOBEC3G. (A) Sequence motifs in Vif implicated in the assembly of a Cul5-E3 ubiquitin ligase complex.
Two conserved domains in Vif, the HCCH motif and the SLQ motif are involved in binding
Cul5 and elongin C (EloC). Vif coordinates one zinc molecule, which may be required
to stabilize a structure important for the binding of cullin 5 (Cul5). (B) Adaptor model for Vif-induced APOBEC3G degradation. According to this model Vif is
an adaptor molecule with binding sites for APOBEC3G and the Cul5-E3 ligase complex
(1). Expression of Vif results in the formation of an APOBEC3G-Vif-E3 ternary complex
(2). This triggers poly-ubiquitination of APOBEC3G (3) resulting in the degradation
of APOBEC3G (4).
Goila-Gaur and Strebel Retrovirology 2008 5:51 doi:10.1186/1742-4690-5-51 |