Endoplasmic reticulum stress in yeast activates not only the UPR but also Rpn4, promoting the clearance of misfolded proteins from the cytosol as part of a modular cross-compartment stress response.
The chaperone protein BiP forms complexes with Ire1 and Perk that dissociate when unfolded proteins bind to BiP to activate the unfolded protein response in the ER.
In parallel to protein-driven processes, characteristic physicochemical properties of the endoplasmic reticulum membrane modulate intracellular fat accumulation and lipid droplet formation.
Endoplasmic reticulum (ER) inheritance regulation during ER stress controls the transmission of misfolded ER proteins from mother to daughter cell in budding yeast.