Endoplasmic Reticulum Stress Induction (None)

Endoplasmic reticulum (ER) stress induction refers to the cellular state and signaling events that occur when the protein-folding capacity of the ER is overwhelmed, leading to an accumulation of unfolded or misfolded proteins within this organelle. The cell initiates adaptive mechanisms collectively known as the unfolded protein response (UPR). If these adaptive responses fail or if the stress persists, prolonged ER stress can trigger programmed cell death (apoptosis). The UPR reduces global protein synthesis, increases production of molecular chaperones to assist in folding, enhances degradation pathways for misfolded proteins (ER-associated degradation), and expands the capacity of the ER. The UPR is mediated by three principal transmembrane sensors located in the ER membrane: IRE1, PERK, and ATF6. These sensors are normally kept inactive by binding with BiP/GRP78/HSPA5 chaperone. Accumulation of unfolded proteins sequesters BiP away from these sensors, allowing their activation.

Other names

ER StressUnfolded Protein Response (UPR)

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