Endoplasmic reticulum association and N-linked glycosylation of the human Nrf3 transcription factor.
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.
Nouhi
Zaynab
Z
Lady Davis Institute for Medical Research, McGill University, Montreal, Quebec, Canada.
Chevillard
Grégory
G
Derjuga
Anna
A
Blank
Volker
V
D000595:Amino Acid Sequence; D000818:Animals; D050976:Basic-Leucine Zipper Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005786:Gene Expression Regulation; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D050976:Basic-Leucine Zipper Transcription Factors; C117963:NFE2L3 protein, human