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. 2017 May 4;7:85. doi: 10.3389/fonc.2017.00085

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Copyright © 2017 Taguchi and Yamamoto.

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) or licensor 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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KEAP1–NRF2 system. KEAP1-CUL3 directly binds NRF2, which is then rapidly degraded by the 26S proteasome in the cytoplasm. NRF2 that escapes KEAP1 trapping is stabilized and accumulates in the nucleus. GSK3 phosphorylates the Neh6 domain of NRF2. Phosphorylated NRF2 binds β-TrCP-CUL1 and is then degraded by the 26S proteasome in the nucleus. NRF2 forms a heterodimer with sMAF and binds CNC-sMAF-binding elements (CsMBE), including the consensus ARE/EpRE sequence, TGACNNNGC. NRF2 upregulates cytoprotective genes encoding antioxidant enzymes and detoxifying enzymes.