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Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress

Endoplasmic reticulum (ER) is a dynamic organelle orchestrating the folding and post-translational maturation of almost all membrane proteins and most secreted proteins. These proteins synthesized in the ER, need to form disulfide bridge to acquire specific three-dimensional structures for function....

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Autores principales: Zhang, Zhe, Zhang, Lu, Zhou, Li, Lei, Yunlong, Zhang, Yuanyuan, Huang, Canhua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6859529/
https://www.ncbi.nlm.nih.gov/pubmed/30470534
http://dx.doi.org/10.1016/j.redox.2018.11.005
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author Zhang, Zhe
Zhang, Lu
Zhou, Li
Lei, Yunlong
Zhang, Yuanyuan
Huang, Canhua
author_facet Zhang, Zhe
Zhang, Lu
Zhou, Li
Lei, Yunlong
Zhang, Yuanyuan
Huang, Canhua
author_sort Zhang, Zhe
collection PubMed
description Endoplasmic reticulum (ER) is a dynamic organelle orchestrating the folding and post-translational maturation of almost all membrane proteins and most secreted proteins. These proteins synthesized in the ER, need to form disulfide bridge to acquire specific three-dimensional structures for function. The formation of disulfide bridge is mediated via protein disulfide isomerase (PDI) family and other oxidoreductases, which contribute to reactive oxygen species (ROS) generation and consumption in the ER. Therefore, redox regulation of ER is delicate and sensitive to perturbation. Deregulation in ER homeostasis, usually called ER stress, can provoke unfolded protein response (UPR) pathways with an aim to initially restore homeostasis by activating genes involved in protein folding and antioxidative machinery. Over time, however, activated UPR involves a variety of cellular signaling pathways which determine the state and fate of cell in large part (like autophagy, apoptosis, ferroptosis, inflammation, senescence, stemness, and cell cycle, etc.). This review will describe the regulation of UPR from the redox perspective in controlling the cell survival or death, emphasizing the redox modifications of UPR sensors/transducers in the ER.
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spelling pubmed-68595292019-11-22 Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress Zhang, Zhe Zhang, Lu Zhou, Li Lei, Yunlong Zhang, Yuanyuan Huang, Canhua Redox Biol Article Endoplasmic reticulum (ER) is a dynamic organelle orchestrating the folding and post-translational maturation of almost all membrane proteins and most secreted proteins. These proteins synthesized in the ER, need to form disulfide bridge to acquire specific three-dimensional structures for function. The formation of disulfide bridge is mediated via protein disulfide isomerase (PDI) family and other oxidoreductases, which contribute to reactive oxygen species (ROS) generation and consumption in the ER. Therefore, redox regulation of ER is delicate and sensitive to perturbation. Deregulation in ER homeostasis, usually called ER stress, can provoke unfolded protein response (UPR) pathways with an aim to initially restore homeostasis by activating genes involved in protein folding and antioxidative machinery. Over time, however, activated UPR involves a variety of cellular signaling pathways which determine the state and fate of cell in large part (like autophagy, apoptosis, ferroptosis, inflammation, senescence, stemness, and cell cycle, etc.). This review will describe the regulation of UPR from the redox perspective in controlling the cell survival or death, emphasizing the redox modifications of UPR sensors/transducers in the ER. Elsevier 2018-11-14 /pmc/articles/PMC6859529/ /pubmed/30470534 http://dx.doi.org/10.1016/j.redox.2018.11.005 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Zhe
Zhang, Lu
Zhou, Li
Lei, Yunlong
Zhang, Yuanyuan
Huang, Canhua
Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
title Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
title_full Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
title_fullStr Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
title_full_unstemmed Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
title_short Redox signaling and unfolded protein response coordinate cell fate decisions under ER stress
title_sort redox signaling and unfolded protein response coordinate cell fate decisions under er stress
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6859529/
https://www.ncbi.nlm.nih.gov/pubmed/30470534
http://dx.doi.org/10.1016/j.redox.2018.11.005
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