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Endoplasmic reticulum association and N‐linked glycosylation of the human Nrf3 transcription factor
Author(s) -
Nouhi Zaynab,
Chevillard Grégory,
Derjuga Anna,
Blank Volker
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.10.041
Subject(s) - endoplasmic reticulum , cycloheximide , transcription factor , proteasome , leucine zipper , glycosylation , activating transcription factor , microbiology and biotechnology , chemistry , atf3 , protein biosynthesis , stim1 , unfolded protein response , biology , biochemistry , gene , promoter , gene expression
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 modification of Nrf3.