A genetic screen identifies a lipid pathway which impacts the endoplasmic reticulum unfolded protein response and highlights a mechanism through which lipid disequilibrium might facilitate the progression of proteopathic diseases.

MCTP is a novel presynaptic calcium sensor, resident within the endoplasmic reticulum, that is required for normal baseline neurotransmission, short-term synaptic plasticity and presynaptic homeostatic plasticity.

A unique form of regulation has been observed in the unfolded protein response of S. pombe, along with a novel mechanism of post-transcriptional mRNA processing.

Restoration of endoplasmic reticulum (ER) homeostatis occurs when levels of the key ER resident chaperone BiP exceed those of accumulating ER clients.

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

Tuning of BiP activity by Fic-mediated AMPylation is required for Drosophila photoreceptor plasticity and attenuation of the unfolded protein response.

GRAMD1 proteins sense a transient expansion of the accessible pool of plasma membrane cholesterol and facilitate its transport to the endoplasmic reticulum at ER-PM contact sites.

Astrocytic ER calcium release and gap junction communication exhibit circadian modulation driven by HERPUD1, highlighting the importance of astrocytic circadian rhythms in brain function.

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

A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.