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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
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Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism

Kit I. Tong
  • Graduate School of Comprehensive Human Sciences, Center for Tsukuba Advanced Research Alliance and JST-ERATO Environmental Response Project, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8577, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Akira Kobayashi
  • Graduate School of Comprehensive Human Sciences, Center for Tsukuba Advanced Research Alliance and JST-ERATO Environmental Response Project, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8577, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Fumiki Katsuoka
  • Graduate School of Comprehensive Human Sciences, Center for Tsukuba Advanced Research Alliance and JST-ERATO Environmental Response Project, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8577, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Masayuki Yamamoto
  • Graduate School of Comprehensive Human Sciences, Center for Tsukuba Advanced Research Alliance and JST-ERATO Environmental Response Project, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8577, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.164

Abstract

Cells are equipped with a number of transcriptional factors that safeguard against various environmental insults. Proteasomal protein degradation plays an important role in the Keap1-Nrf2 cytoprotection system, with molecular machinery similar to that for other environmental defense systems such as inflammatory and hypoxic responses. While Nrf2 protein stabilization is known to be redox-sensitive, the transcription factors NF-κB and HIF-1α for inflammatory and hypoxic responses, respectively, are also influenced by the cellular redox conditions. In this review we present the recently proposed two-site substrate recognition model of the Keap1-Nrf2 system, which regulates the cellular responses against oxidative and xenobiotic stresses. The implications of two destructive motifs in Nrf2, the ETGE and DLG motifs, which appear to function as a hinge and latch attenuating Keap1 activity in different redox states, are discussed.

Keywords: CUL3-BTB E3 ligase; DLG motif; ETGE motif; Keap1; Nrf2; oxidative stress sensor

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Corresponding author


Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, Volume 387, Issue 10/11, Pages 1311–1320, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.164.

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