The Unfolded Protein Response: An Overview
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 unfol...
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doaj-b02c4b0686ab4bcda3258a728335c4512021-04-29T23:00:41ZengMDPI AGBiology2079-77372021-04-011038438410.3390/biology10050384The Unfolded Protein Response: An OverviewAdam Read0Martin Schröder1Department of Biosciences, Durham University, South Road, Durham DH1 3LE, UKDepartment of Biosciences, Durham University, South Road, Durham DH1 3LE, UKThe 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 <i>Saccharomyces cerevisiae</i>. This pathway involves spliceosome independent splicing of <i>HAC1</i> or <i>XBP1</i> 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 NH<sub>2</sub> 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.https://www.mdpi.com/2079-7737/10/5/384UPRIRE1PERKATF6RIDDERAD |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Adam Read Martin Schröder |
spellingShingle |
Adam Read Martin Schröder The Unfolded Protein Response: An Overview Biology UPR IRE1 PERK ATF6 RIDD ERAD |
author_facet |
Adam Read Martin Schröder |
author_sort |
Adam Read |
title |
The Unfolded Protein Response: An Overview |
title_short |
The Unfolded Protein Response: An Overview |
title_full |
The Unfolded Protein Response: An Overview |
title_fullStr |
The Unfolded Protein Response: An Overview |
title_full_unstemmed |
The Unfolded Protein Response: An Overview |
title_sort |
unfolded protein response: an overview |
publisher |
MDPI AG |
series |
Biology |
issn |
2079-7737 |
publishDate |
2021-04-01 |
description |
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 <i>Saccharomyces cerevisiae</i>. This pathway involves spliceosome independent splicing of <i>HAC1</i> or <i>XBP1</i> 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 NH<sub>2</sub> 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. |
topic |
UPR IRE1 PERK ATF6 RIDD ERAD |
url |
https://www.mdpi.com/2079-7737/10/5/384 |
work_keys_str_mv |
AT adamread theunfoldedproteinresponseanoverview AT martinschroder theunfoldedproteinresponseanoverview AT adamread unfoldedproteinresponseanoverview AT martinschroder unfoldedproteinresponseanoverview |
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