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

FEBS Lett. 2007 Nov 27;581(28):5401-6. doi: 10.1016/j.febslet.2007.10.041. Epub 2007 Oct 30.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Basic-Leucine Zipper Transcription Factors / chemistry
  • Basic-Leucine Zipper Transcription Factors / genetics
  • Basic-Leucine Zipper Transcription Factors / metabolism*
  • Cell Line
  • Endoplasmic Reticulum / metabolism*
  • Gene Expression Regulation
  • Glycosylation
  • Humans
  • Molecular Sequence Data
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Basic-Leucine Zipper Transcription Factors
  • NFE2L3 protein, human