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. 2021 Sep 24;15:739506. doi: 10.3389/fncel.2021.739506

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Copyright © 2021 Wu, Liu, Li, Zhou, Huang, Wu, Zhan and Shen.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The transcription factor nuclear factor erythroid-derived 2-like 2 (Nrf2) plays an important role in cellular antioxidant and other important physiological processes. Under physiological conditions, Nrf2 can be ubiquitinated and bind to Keap1. Subsequently, Nrf2 can be degraded by keAP1-dependent proteasome. In addition to ubiquitination, various post-translational modifications such as phosphorylation can affect the stability of Nrf2 structure. Under moderate oxidative stress and antioxidant stimulation, Nrf2 can enhance its stability through various post-translational modifications such as phosphorylation. At the same time, Nrf2 with enhanced stability can be translocated to the nucleus and combined with the cis-acting element ARE to activate the transcription of antioxidant genes.