Emerin, a protein that plays key roles in nuclear organization, can be dynamically degraded in response to environmental stimuli such as ER stress.

Sphingolipids govern the compartmentalization of yeast cells through the assembly of lateral diffusion barriers in ER membranes.

mTORC1 inhibition by perinatal ER stress induces beta-cell growth arrest with subsequent development of diabetes.

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.

Ceapins specifically inhibit ATF6α signaling by preventing its transport to the Golgi during endoplasmic reticulum stress.

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.

LRH-1/NR5A2 responds to ER stress by inducing a novel pathway that is required for stress resolution in mice and can be targeted by LRH-1 agonists.

C53 bridges selective autophagy with ribosome-associated quality control at the endoplasmic reticulum.

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.