ATF6 is an ER stress‑responsive transcription factor that enhances protein‑folding capacity and strengthens ER‑associated degradation. After trafficking to the Golgi and undergoing regulated proteolysis, ATF6 activates genes that restore ER proteostasis during unfolded protein accumulation.
ER stress arises when misfolded proteins accumulate in the endoplasmic reticulum, overwhelming its folding capacity. Through IRE1, PERK and ATF6 signalling, the unfolded protein response restores proteostasis, reduces protein load and protects cells from stress‑induced damage.
The unfolded protein response (UPR) is a conserved ER stress pathway that detects misfolded proteins and restores proteostasis. Through IRE1, PERK and ATF6 signalling, cells expand folding capacity, reduce protein load and maintain homeostasis under conditions of ER stress.
ATF6 is an ER stress‑responsive transcription factor that enhances protein‑folding capacity and strengthens ER‑associated degradation. After trafficking to the Golgi and undergoing regulated proteolysis, ATF6 activates genes that restore ER proteostasis during unfolded protein accumulation.
ER stress arises when misfolded proteins accumulate in the endoplasmic reticulum, overwhelming its folding capacity. Through IRE1, PERK and ATF6 signalling, the unfolded protein response restores proteostasis, reduces protein load and protects cells from stress‑induced damage.
The unfolded protein response (UPR) is a conserved ER stress pathway that detects misfolded proteins and restores proteostasis. Through IRE1, PERK and ATF6 signalling, cells expand folding capacity, reduce protein load and maintain homeostasis under conditions of ER stress.
