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. 2019 Dec 30;12(1):95. doi: 10.3390/cancers12010095

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

A model of NF-E2 p45-related factor 2 (NRF2) deregulation by Promyelocytic leukemia/retinoic acid receptor α (PML/RARa). (a) NRF2 activity is maintained at a low level via Keap1 binding, constitutive ubiquitination and proteosomal degradation. Electrophiles and oxidants inhibit its degradation, enabling NRF2 protein to accumulate in the nucleus initiating a genetic program to allow cellular adaptation to stress. (b) PML/RARa binds to NRF2 protein, segregates it to the cytoplasm, accelerates its degradation, and impedes its upregulation and induction of (antioxidant response elements) ARE-driven genes in response to electrophiles and oxidants; therefore, NRF2 function in response to ROS accumulation is insufficient.