NRF2, a Key Regulator of Antioxidants with Two Faces towards Cancer

Figure 3

Interaction of NRF2 and KEAP1: hinge and latch model. KEAP1 proteins dimerize via BTB domains. The KEAP1 homodimer identifies the DLG (weak interaction) and ETGE (strong interaction) motifs in the NRF2. NRF2 tightly binds to KEAP1 homodimer in basal state. After stress, weaker DLG motif is detached, blocking ubiquitination of NRF2 and facilitating nuclear import and binding to ARE. BTB: Broad Complex, Tramtrack, and Bric-a-Brac, IVR: intervening region, DGR: double glycine repeat (=Kelch), and ARE: antioxidant response element.