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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  Junyu Xiao  Chih-chen Wang  Lei Wang  
【摘要】:Reversible phosphorylation is one of the most prevalent processes to affect protein conformation,localization and degradation.Family with sequence similarity 20 C(Fam20 C),the physiological Golgi casein kinase,phosphorylates numerous secreted proteins that are involved in a wide variety of biological processes.However,little is known about the role of protein phosphorylation in the lumen of the secretory pathway.Here we show that that Fam20 C interacts with many luminal proteins and that its depletion results in a more reduced ER.We further show that Ero1α,the pivotal sulfhydryl oxidase in the ER,is transported to the Golgi apparatus and phosphorylated by Fam20 C at Ser145.Phosphorylated Ero1α can be retrograde transported to the ER mediated by ERp44/KDEL receptor.Importantly,phosphorylated Ero1α displays enhanced oxidase activity and accelerates oxidative protein folding.Phosphorylation of Ero1α Ser145 is critical for maintaining the ER redox homeostasis,and is induced under hypoxia,reductive stress and mammalian lactation.Our study expands Fam20 C's biological roles in the ER lumen and for the first time establishes the link between secretory protein phosphorylation and oxidative protein folding.

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