Ontology highlight
ABSTRACT:
SUBMITTER: Brown M
PROVIDER: S-EPMC7851869 | biostudies-literature | 2020 Nov
REPOSITORIES: biostudies-literature
Brown Max M Dainty Samantha S Strudwick Natalie N Mihai Adina D AD Watson Jamie N JN Dendooven Robina R Paton Adrienne W AW Paton James C JC Schröder Martin M
Molecular biology of the cell 20200902 23
Accumulation of unfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates a signaling network known as the unfolded protein response (UPR). Here we characterize how ER stress and the UPR inhibit insulin signaling. We find that ER stress inhibits insulin signaling by depleting the cell surface population of the insulin receptor. ER stress inhibits proteolytic maturation of insulin proreceptors by interfering with transport of newly synthesized insulin proreceptors from th ...[more]