Proteins of the reticulon and REEP families, homologous to the products of human Hereditary Spastic Paraplegia disease genes, contribute to shaping and continuity of the axonal endoplasmic reticulum network in Drosophila.

Stress sensors in the membrane of the endoplasmic reticulum respond to the accumulation of unfolded proteins by briefly forming small phosphorylation-competent oligomers and dissolving back into active dimers.

Interaction mapping of ubiquitin ligase complexes embedded in the endoplasmic reticulum membrane has identified interactors of RNF26 that influence innate immune signalling.

Signaling function of sigma 1 receptor is related to its ability to organize cholesterol-enriched microdomains in the endoplasmic reticulum membrane.

Endoplasmic reticulum-associated degradation (ERAD) is a critical protein quality control checkpoint for thymocyte β-slection.

Selective docking of HAC1 mRNA on Ire1 clusters at a site separate from the Ire1 RNase domain is key for endoplasmic reticulum stress signaling.

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

A post-lysosomal cholesterol transport inhibitor reveals how the endoplasmic reticulum membrane regulates total cellular cholesterol by constantly monitoring a critical pool of cholesterol in the plasma membrane.

Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.

Adapting a cytosolic enzyme that breaks down glutathione to function in the lumen of the endoplasmic reticulum challenges the long-held view that reduced glutathione fuels disulfide rearrangements during protein folding.