Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity

Stress in the endoplasmic reticulum (ER) triggers the unfolded protein response (UPR), a signaling mechanism that allows cellular adaptation to ER stress by engaging pro-adaptive transcription factors and alleviating protein folding demand. One such transcription factor, X-box binding protein (XBP1)...

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Main Authors: Joseph W. Brewer, Andrew E. Byrd
Format: Article
Language:English
Published: MDPI AG 2012-10-01
Series:Cells
Subjects:
Online Access:http://www.mdpi.com/2073-4409/1/4/738
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author Joseph W. Brewer
Andrew E. Byrd
author_facet Joseph W. Brewer
Andrew E. Byrd
author_sort Joseph W. Brewer
collection DOAJ
description Stress in the endoplasmic reticulum (ER) triggers the unfolded protein response (UPR), a signaling mechanism that allows cellular adaptation to ER stress by engaging pro-adaptive transcription factors and alleviating protein folding demand. One such transcription factor, X-box binding protein (XBP1), originates from the inositol-requiring transmembrane kinase/endoribonuclease 1 (IRE1) UPR stress sensor. XBP1 up-regulates a pool of genes involved in ER protein translocation, protein folding, vesicular trafficking and ER- associated protein degradation. Recent data suggest that the regulation of XBP1 expression and transcriptional activity may be a tissue- and stress-dependent phenomenon. Moreover, the intricacies involved in “fine-tuning” XBP1 activity in various settings are now coming to light. Here, we provide an overview of recent developments in understanding the regulatory mechanisms underlying XBP1 expression and activity and discuss the significance of these new insights.
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spelling doaj.art-ad9278ff0d31444fb54e8691806a73da2023-09-02T23:54:23ZengMDPI AGCells2073-44092012-10-011473875310.3390/cells1040738Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and ActivityJoseph W. BrewerAndrew E. ByrdStress in the endoplasmic reticulum (ER) triggers the unfolded protein response (UPR), a signaling mechanism that allows cellular adaptation to ER stress by engaging pro-adaptive transcription factors and alleviating protein folding demand. One such transcription factor, X-box binding protein (XBP1), originates from the inositol-requiring transmembrane kinase/endoribonuclease 1 (IRE1) UPR stress sensor. XBP1 up-regulates a pool of genes involved in ER protein translocation, protein folding, vesicular trafficking and ER- associated protein degradation. Recent data suggest that the regulation of XBP1 expression and transcriptional activity may be a tissue- and stress-dependent phenomenon. Moreover, the intricacies involved in “fine-tuning” XBP1 activity in various settings are now coming to light. Here, we provide an overview of recent developments in understanding the regulatory mechanisms underlying XBP1 expression and activity and discuss the significance of these new insights.http://www.mdpi.com/2073-4409/1/4/738endoplasmic reticulumendoplasmic reticulum stressunfolded protein responseXBP1
spellingShingle Joseph W. Brewer
Andrew E. Byrd
Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity
Cells
endoplasmic reticulum
endoplasmic reticulum stress
unfolded protein response
XBP1
title Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity
title_full Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity
title_fullStr Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity
title_full_unstemmed Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity
title_short Intricately Regulated: A Cellular Toolbox for Fine-Tuning XBP1 Expression and Activity
title_sort intricately regulated a cellular toolbox for fine tuning xbp1 expression and activity
topic endoplasmic reticulum
endoplasmic reticulum stress
unfolded protein response
XBP1
url http://www.mdpi.com/2073-4409/1/4/738
work_keys_str_mv AT josephwbrewer intricatelyregulatedacellulartoolboxforfinetuningxbp1expressionandactivity
AT andrewebyrd intricatelyregulatedacellulartoolboxforfinetuningxbp1expressionandactivity