Cellular stress induced by the abnormal accumulation of unfolded or misfolded proteins at
the endoplasmic reticulum (ER) is emerging as a possible driver of human diseases,
including cancer, diabetes, obesity and neurodegeneration. ER proteostasis surveillance is
mediated by the unfolded protein response (UPR), a signal transduction pathway that
senses the fidelity of protein folding in the ER lumen. The UPR transmits information about
protein folding status to the nucleus and cytosol to adjust the protein folding capacity of the …

The unfolded protein response (UPR) comprises a network of signalling pathways that
reprogramme transcription, translation and protein modifications to relieve the load of
unfolded or misfolded proteins in the endoplasmic reticulum lumen and restore proteostasis.
Understanding the regulation of the UPR and the role it has in the pathophysiology of
various cell types and organs might open new therapeutic avenues. Cellular stress induced
by the abnormal accumulation of unfolded or misfolded proteins at the endoplasmic …