Dataset Information

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

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 at Ser145 under reductive stress and under secretion-demanding conditions, such as mammalian lactation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Cervix Carcinoma

SUBMITTER: Jianchao Zhang

LAB HEAD: Lei Wang

PROVIDER: PXD009333 | Pride | 2018-05-30

REPOSITORIES: Pride

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Publications

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

Zhang Jianchao J Zhu Qinyu Q Wang Xi'e X Yu Jiaojiao J Chen Xinxin X Wang Jifeng J Wang Xi X Xiao Junyu J Wang Chih-Chen CC Wang Lei L

The EMBO journal 20180601 14

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 o ...[more]

PMID: 29858230

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Dataset Information

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

Publications

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

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