Molecular and Cellular Control of the Nrf1 Transcription Factor
An Integral Membrane Glycoprotein
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This study has revealed that Nrf1 is an integralmembrane glycoprotein with transmembrane andextramembrane regions, located in both theendoplasmic reticulum (ER) and the nuclear envelope.This CNC/bZIP protein is targeted and anchored in theER through its N-terminal Homology Box 1 (NHB1)sequence, and in the ER lumen it is glycosylated byamide-linked attachment of glycans to the asparagineswithin its NST domain. After being correctly foldedinto a proper topology, mature Nrf1 protein could besorted out into the nuclear envelope. Once reachingthe inner nuclear membrane, it can gain access to thepro...
This study has revealed that Nrf1 is an integral
membrane glycoprotein with transmembrane and
extramembrane regions, located in both the
endoplasmic reticulum (ER) and the nuclear envelope.
This CNC/bZIP protein is targeted and anchored in the
ER through its N-terminal Homology Box 1 (NHB1)
sequence, and in the ER lumen it is glycosylated by
amide-linked attachment of glycans to the asparagines
within its NST domain. After being correctly folded
into a proper topology, mature Nrf1 protein could be
sorted out into the nuclear envelope. Once reaching
the inner nuclear membrane, it can gain access to the
promoter regions of its target genes and relevant
transcriptional mechineries in the nucleoplasm. It
should be noted that, although Nrf1 is integrated in
the ER membrane, it is not activated by ER stressors,
and conversely,they were found
to inhibit activation of this factor by a redox
inducer tBHQ. Therefore, Nrf1 may function
essentially as a control of redox compartmentization
for maintaining redox homeostasis between the ER and
nucleus; the former is a more oxidizing environment
in the cell, whereas the latter is a more reducing
conpartment.
membrane glycoprotein with transmembrane and
extramembrane regions, located in both the
endoplasmic reticulum (ER) and the nuclear envelope.
This CNC/bZIP protein is targeted and anchored in the
ER through its N-terminal Homology Box 1 (NHB1)
sequence, and in the ER lumen it is glycosylated by
amide-linked attachment of glycans to the asparagines
within its NST domain. After being correctly folded
into a proper topology, mature Nrf1 protein could be
sorted out into the nuclear envelope. Once reaching
the inner nuclear membrane, it can gain access to the
promoter regions of its target genes and relevant
transcriptional mechineries in the nucleoplasm. It
should be noted that, although Nrf1 is integrated in
the ER membrane, it is not activated by ER stressors,
and conversely,they were found
to inhibit activation of this factor by a redox
inducer tBHQ. Therefore, Nrf1 may function
essentially as a control of redox compartmentization
for maintaining redox homeostasis between the ER and
nucleus; the former is a more oxidizing environment
in the cell, whereas the latter is a more reducing
conpartment.
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