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Evolutionary conserved N-terminal domain of Nrf2 is essential for the Keap1-mediated degradation of the protein by proteasome.

Abstract：

:Under homeostatic conditions, Nrf2 activity is constitutively repressed. This process is dependent on Keap1, to which Nrf2 binds through the Neh2 domain. Since the N-terminal subdomain of Neh2 (Neh2-NT) contains evolutionarily conserved motifs, we examined the roles they play in the degradation of Nrf2. In Neh2-NT, we defined a novel motif that is distinct from the previously characterized DIDLID motif and designated it DLG motif. Deletion of Neh2-NT or mutation of the DLG motif largely abolished the Keap1-mediated degradation of Nrf2. These mutations were found to enfeeble the binding affinity of Nrf2 to Keap1. The Neh2-NT subdomain directed DLG-dependent, Keap1-independent, degradation of a reporter protein in the nucleus. By contrast, mutation of DLG did not affect the half-life of native Nrf2 protein in the nucleus under oxidative stress conditions. These results thus demonstrate that DLG motif plays essential roles in the Keap1-mediated proteasomal degradation of Nrf2 in the cytoplasm.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Katoh Y,Iida K,Kang MI,Kobayashi A,Mizukami M,Tong KI,McMahon M,Hayes JD,Itoh K,Yamamoto M

doi

10.1016/j.abb.2004.10.012

subject

Has Abstract

pub_date

2005-01-15 00:00:00

pages

342-50

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(04)00571-5

journal_volume

433

pub_type

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