Endoplasmic reticulum association and N-linked glycosylation of the human Nrf3 transcription factor

被引：66

作者：

Nouhi, Zaynab ^{[1
,2
]}

Chevillard, Gory ^{[1
,2
]}

Derjuga, Anna ^{[1
]}

Blank, Volker ^{[1
,2
,3
]}

机构：

[1] McGill Univ, Lady Davis Inst Med Res, Montreal, PQ H3T 1E2, Canada

[2] McGill Univ, Dept Med, Div Expt Med, Montreal, PQ, Canada

[3] McGill Univ, Dept Physiol, Montreal, PQ, Canada

来源：

FEBS LETTERS | 2007年 / 581卷 / 28期

关键词：

Nrf3; glycosylation; MG-132; tunicamycin; thapsigargin; ER-associated protein;

D O I：

10.1016/j.febslet.2007.10.041

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

We have analysed the molecular and cellular regulation of the basic-leucine zipper (bZIP) transcription factor Nrf3 (NFE2-Related Factor 3). Cycloheximide studies revealed a rapid turnover of Nrf3. We showed that the proteasome inhibitor MG-132 increases Nrf3 protein levels. Furthermore, we demonstrated that Nrf3 is an N-glycosylated protein associated with the endoplasmic reticulum. Thus, our studies provide the first evidence of a post-translational modi. cation of Nrf3. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：5401 / 5406

页数：6

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