Fam20C interactome in the secretory pathway under ER stress

ABSTRACT: Accumulated unfolded proteins in the endoplasmic reticulum (ER) will trigger the unfolded protein response (UPR) to increase protein-folding capacity. The ER proteostasis and UPR signaling should be precisely and timely regulated. In the project, by unbiased proteomics analysis, we identify that the serine 357 of protein disulfide isomerase (PDI) is rapidly phosphorylated by the secretory pathway kinase Fam20C under ER stress. Remarkably, phosphorylated Ser357 induces an open conformation of PDI and turns it from a ‘foldase’ to a ‘holdase’, which is critical for preventing protein misfolding in the ER.

OTHER RELATED OMICS DATASETS IN: MODEL1109130000 MODEL1909260003 MODEL1909260004 MODEL1703310000 MODEL1909260005 MODEL1909260006 MODEL1311110000 MODEL1311110001

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte, Cell Culture

SUBMITTER: Jianchao Zhang  

LAB HEAD: Lei Wang

PROVIDER: PXD016619 | Pride | 2020-03-02

REPOSITORIES: Pride