A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability

A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability

DDRGK1 is an ER membrane protein that is subject to Ufm1 modification, but its function in ER homeostasis is unknown. Here, the authors show that ufmylated DDRGK1 interacts with and stabilizes the ER-stress sensor protein IRE1a, in turn repressing ER stress and apoptosis.

Bibliographic Details
Main Authors: Jiang Liu, Ying Wang, Lizhi Song, Linghua Zeng, Weiwei Yi, Ting Liu, Huanzhen Chen, Miao Wang, Zhenyu Ju, Yu-Sheng Cong
Format: Article
Language:English
Published: Nature Publishing Group 2017-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms14186
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spelling doaj-f947839b8b534eb288d8307e574f55e82021-05-11T07:57:53ZengNature Publishing GroupNature Communications2041-17232017-01-018111210.1038/ncomms14186A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stabilityJiang Liu0Ying Wang1Lizhi Song2Linghua Zeng3Weiwei Yi4Ting Liu5Huanzhen Chen6Miao Wang7Zhenyu Ju8Yu-Sheng Cong9Institute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityDepartment of Cardiology, The First Hospital of Shanxi Medical UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityInstitute of Aging Research, School of Medicine, Hangzhou Normal UniversityDDRGK1 is an ER membrane protein that is subject to Ufm1 modification, but its function in ER homeostasis is unknown. Here, the authors show that ufmylated DDRGK1 interacts with and stabilizes the ER-stress sensor protein IRE1a, in turn repressing ER stress and apoptosis.https://doi.org/10.1038/ncomms14186
collection DOAJ
language English
format Article
sources DOAJ
author Jiang Liu
Ying Wang
Lizhi Song
Linghua Zeng
Weiwei Yi
Ting Liu
Huanzhen Chen
Miao Wang
Zhenyu Ju
Yu-Sheng Cong
spellingShingle Jiang Liu
Ying Wang
Lizhi Song
Linghua Zeng
Weiwei Yi
Ting Liu
Huanzhen Chen
Miao Wang
Zhenyu Ju
Yu-Sheng Cong
A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability
Nature Communications
author_facet Jiang Liu
Ying Wang
Lizhi Song
Linghua Zeng
Weiwei Yi
Ting Liu
Huanzhen Chen
Miao Wang
Zhenyu Ju
Yu-Sheng Cong
author_sort Jiang Liu
title A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability
title_short A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability
title_full A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability
title_fullStr A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability
title_full_unstemmed A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability
title_sort critical role of ddrgk1 in endoplasmic reticulum homoeostasis via regulation of ire1α stability
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-01-01
description DDRGK1 is an ER membrane protein that is subject to Ufm1 modification, but its function in ER homeostasis is unknown. Here, the authors show that ufmylated DDRGK1 interacts with and stabilizes the ER-stress sensor protein IRE1a, in turn repressing ER stress and apoptosis.
url https://doi.org/10.1038/ncomms14186
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