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Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders

Misfolded proteins retained in the endoplasmic reticulum cause many human diseases. ER-associated degradation (ERAD) is one of the protein quality and quantity control system located at ER, which is responsible for translocating the misfolded proteins or properly folded but excess proteins out of th...

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Autores principales: Luo, Hui, Jiao, Qibin, Shen, Chuanbin, Shao, Chenyi, Xie, Jinyan, Chen, Yue, Feng, Xinglin, Zhang, Xingwei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10339828/
https://www.ncbi.nlm.nih.gov/pubmed/37455916
http://dx.doi.org/10.3389/fendo.2023.1123769
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author Luo, Hui
Jiao, Qibin
Shen, Chuanbin
Shao, Chenyi
Xie, Jinyan
Chen, Yue
Feng, Xinglin
Zhang, Xingwei
author_facet Luo, Hui
Jiao, Qibin
Shen, Chuanbin
Shao, Chenyi
Xie, Jinyan
Chen, Yue
Feng, Xinglin
Zhang, Xingwei
author_sort Luo, Hui
collection PubMed
description Misfolded proteins retained in the endoplasmic reticulum cause many human diseases. ER-associated degradation (ERAD) is one of the protein quality and quantity control system located at ER, which is responsible for translocating the misfolded proteins or properly folded but excess proteins out of the ER for proteasomal degradation. Recent studies have revealed that mice with ERAD deficiency in specific cell types exhibit impaired metabolism homeostasis and metabolic diseases. Here, we highlight the ERAD physiological functions in metabolic disorders in a substrate-dependent and cell type-specific manner.
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spelling pubmed-103398282023-07-14 Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders Luo, Hui Jiao, Qibin Shen, Chuanbin Shao, Chenyi Xie, Jinyan Chen, Yue Feng, Xinglin Zhang, Xingwei Front Endocrinol (Lausanne) Endocrinology Misfolded proteins retained in the endoplasmic reticulum cause many human diseases. ER-associated degradation (ERAD) is one of the protein quality and quantity control system located at ER, which is responsible for translocating the misfolded proteins or properly folded but excess proteins out of the ER for proteasomal degradation. Recent studies have revealed that mice with ERAD deficiency in specific cell types exhibit impaired metabolism homeostasis and metabolic diseases. Here, we highlight the ERAD physiological functions in metabolic disorders in a substrate-dependent and cell type-specific manner. Frontiers Media S.A. 2023-06-29 /pmc/articles/PMC10339828/ /pubmed/37455916 http://dx.doi.org/10.3389/fendo.2023.1123769 Text en Copyright © 2023 Luo, Jiao, Shen, Shao, Xie, Chen, Feng and Zhang https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Endocrinology
Luo, Hui
Jiao, Qibin
Shen, Chuanbin
Shao, Chenyi
Xie, Jinyan
Chen, Yue
Feng, Xinglin
Zhang, Xingwei
Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
title Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
title_full Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
title_fullStr Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
title_full_unstemmed Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
title_short Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
title_sort unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
topic Endocrinology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10339828/
https://www.ncbi.nlm.nih.gov/pubmed/37455916
http://dx.doi.org/10.3389/fendo.2023.1123769
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