Abstract:The cellular abundance of the redox‐sensitive transcription factor Nrf2 is controlled by Keap1, an inhibitory protein that functions as a substrate adaptor for ubiquitylation of Nrf2 by the Cullin3/RING box1 (Cul3‐Rbx1) E3 ubiquitin ligase complex, thereby targeting Nrf2 for proteasome‐dependent degradation in the cytoplasm. Nrf2 can also be degraded in the nucleus but mechanistic details are lacking. Here, we show that promyelocytic leukemia‐nuclear body (PML‐NB)‐enriched preparations of HepG2 cells treated w… Show more
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