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Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α, EMBO J, 1 June 2018
2018-05-07 | 【     】【打印】【关闭

NEMBO J, 1 June 2018,DOI: 10.15252/embj.201798699

Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α

Jianchao Zhang, Qinyu Zhu, Xi'e Wang, Jiaojiao Yu, Xinxin Chen, Jifeng Wang, Xi Wang, Chih‐chen Wang, Lei Wang

Abstract

Family with sequence similarity 20C (Fam20C), the physiological Golgi casein kinase, phosphorylates numerous secreted proteins that are involved in a wide variety of biological processes. However, the role of Fam20C in regulating proteins in the endoplasmic reticulum (ER) lumen is largely unknown. Here, we report that Fam20C interacts with various luminal proteins and that its depletion results in a more reduced ER lumen. We further show that ER oxidoreductin 1α (Ero1α), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde‐transported to the ER mediated by ERp44. The phosphorylation of Ser145 greatly enhances Ero1α oxidase activity and is critical for maintaining ER redox homeostasis and promoting oxidative protein folding. Notably, phosphorylation of Ero1α is induced under hypoxia, reductive stress, and secretion‐demanding conditions such as mammalian lactation. Collectively, our findings open a door to uncover how oxidative protein folding is regulated by phosphorylation in the secretory pathway.

文章链接:http://emboj.embopress.org/content/early/2018/06/01/embj.201798699

相关报道:http://www.ibp.cas.cn/kyjz/zxdt/201806/t20180604_5021147.html

 

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