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...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:EMBO J
Päätekijät: Yu, Jiaojiao, Li, Tao, Liu, Yu, Wang, Xi, Zhang, Jianchao, Wang, Xi'e, Shi, Guizhi, Lou, Jizhong, Wang, Likun, Wang, Chih‐chen, Wang, Lei
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: John Wiley and Sons Inc. 2020
Aiheet:
Articles
Linkit: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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