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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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Detaylı Bibliyografya
Yayımlandı:EMBO J
Asıl Yazarlar: Yu, Jiaojiao, Li, Tao, Liu, Yu, Wang, Xi, Zhang, Jianchao, Wang, Xi'e, Shi, Guizhi, Lou, Jizhong, Wang, Likun, Wang, Chih‐chen, Wang, Lei
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: John Wiley and Sons Inc. 2020
Konular:
Online Erişim: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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