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Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress

Accumulated unfolded proteins in the endoplasmic reticulum (ER) trigger the unfolded protein response (UPR) to increase ER protein folding capacity. ER proteostasis and UPR signaling need to be regulated in a precise and timely manner. Here, we identify phosphorylation of protein disulfide isomerase...

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Библиографические подробности
Опубликовано в: :EMBO J
Главные авторы: Yu, Jiaojiao, Li, Tao, Liu, Yu, Wang, Xi, Zhang, Jianchao, Wang, Xi'e, Shi, Guizhi, Lou, Jizhong, Wang, Likun, Wang, Chih‐chen, Wang, Lei
Формат: Artigo
Язык:Inglês
Опубликовано: John Wiley and Sons Inc. 2020
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC7232009/
https://ncbi.nlm.nih.gov/pubmed/32149426
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.15252/embj.2019103841
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