Ontology highlight
ABSTRACT:
SUBMITTER: Amin-Wetzel N
PROVIDER: S-EPMC5733394 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Amin-Wetzel Niko N Saunders Reuben A RA Kamphuis Maarten J MJ Rato Claudia C Preissler Steffen S Harding Heather P HP Ron David D
Cell 20171130 7
When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER-protein-folding capacity to restore protein-folding homeostasis. Unfolded proteins activate UPR signaling across the ER membrane to the nucleus by promoting oligomerization of IRE1, a conserved transmembrane ER stress receptor. However, the coupling of ER stress to IRE1 oligomerization and activation has remained obscure. Here, we report that the ER luminal co-chaperone ERdj4/DNA ...[more]