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

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

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.

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

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.

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.

ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.

Plant reticulons bind Atg8 under ER stress to promote reticulophagy and ameliorate ER stress in the maize endosperm.