Cellular responses to endoplasmic reticulum stress

Abstract

The Endoplasmic reticulum (ER) is a highly dynamic organelle that provides high fidelity quality control in protein synthesis, maturation and transport. The complex function of the ER can be significantly influenced by various factors both inside the cell and in its microenvironment. Disturbances in ER protein folding capacity result in accumulation of misfolded proteins in the ER lumen and in activation of ER stress. The unfolded protein response (UPR) normally has prosurvival functions and protects cells by providing the reestablishment of protein processing and cellular homeostasis. However, prolonged and excessive ER stress results in activation of apoptotic pathways. Dysregulation of ER function has been recognized as a cause of numerous pathophysiological conditions. Therefore, detailed investigation of ER stress signaling during disease may provide promising approaches in the  development of UPR-modifying therapeutic strategies.