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The Unfolded Protein Response: An Overview

Read, Adam; Schröder, Martin

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Authors

Adam Read



Abstract

The unfolded protein response is the mechanism by which cells control endoplasmic reticulum (ER) protein homeostasis. Under normal conditions, the UPR is not activated; however, under certain stresses, such as hypoxia or altered glycosylation, the UPR can be activated due to an accumulation of unfolded proteins. The activation of the UPR involves three signaling pathways, IRE1, PERK and ATF6, which all play vital roles in returning protein homeostasis to levels seen in non-stressed cells. IRE1 is the best studied of the three pathways, as it is the only pathway present in Saccharomyces cerevisiae. This pathway involves spliceosome independent splicing of HAC1 or XBP1 in yeast and mammalians cells, respectively. PERK limits protein synthesis, therefore reducing the number of new proteins requiring folding. ATF6 is translocated and proteolytically cleaved, releasing a NH2 domain fragment which is transported to the nucleus and which affects gene expression. If the UPR is unsuccessful at reducing the load of unfolded proteins in the ER and the UPR signals remain activated, this can lead to programmed cell death.

Citation

Read, A., & Schröder, M. (2021). The Unfolded Protein Response: An Overview. Biology, 10(5), Article 384. https://doi.org/10.3390/biology10050384

Journal Article Type Article
Acceptance Date Apr 27, 2021
Online Publication Date Apr 29, 2021
Publication Date 2021-05
Deposit Date Oct 20, 2021
Publicly Available Date Oct 28, 2022
Journal Biology
Publisher MDPI
Peer Reviewed Peer Reviewed
Volume 10
Issue 5
Article Number 384
DOI https://doi.org/10.3390/biology10050384

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http://creativecommons.org/licenses/by/4.0/

Copyright Statement
© 2021 by the authors.
Licensee MDPI, Basel, Switzerland.
This article is an open access article
distributed under the terms and
conditions of the Creative Commons
Attribution (CC BY) license (https://
creativecommons.org/licenses/by)





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