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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Gepubliceerd in:EMBO J
Hoofdauteurs: Yu, Jiaojiao, Li, Tao, Liu, Yu, Wang, Xi, Zhang, Jianchao, Wang, Xi'e, Shi, Guizhi, Lou, Jizhong, Wang, Likun, Wang, Chih‐chen, Wang, Lei
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: John Wiley and Sons Inc. 2020
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Articles
Online toegang: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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