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

fmo-4 slows aging downstream of dietary restriction and mTOR and regulates calcium-mediated signaling in the hypodermis.

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.

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

In parallel to protein-driven processes, characteristic physicochemical properties of the endoplasmic reticulum membrane modulate intracellular fat accumulation and lipid droplet formation.

Feedback mechanisms that contribute to the deactivation of the unfolded protein response lead to the dysregulation of mRNA expression during chronic stress in the liver, including that of the critical endoplasmic reticulum chaperone BiP.

When non-glycosylated, Seipin, which spans the endoplasmic reticulum (ER) membrane twice, forms aggregates in an oligomerization-dependent manner, distorts the shape of the ER, and incorporates SERCA2b via direct interaction, inactivation of which results in induction of ER stress and apoptosis.

Celastrol covalently inhibited the chaperone activity of GRP78 and could disconnect the transduction of ER stress signal to downstream inflammatory response and lipid metabolism.

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

Endoplasmic reticulum (ER) inheritance regulation during ER stress controls the transmission of misfolded ER proteins from mother to daughter cell in budding yeast.