Review of ER stress and unfolded protein response

Abstract

The cell is the fundamental unit of life, and all of the organelles within it perform essential tasks. Cells must meet their typical requirements for survival and development in order to contribute to the functioning of living things. Protein folding in the rough ER, the major organelle for the synthesis, folding, and modification of secreted and transmembrane proteins, is essential for their proper function in the cytoplasm. Endoplasmic reticulum stress (ERS) occurs when the protein-folding capacity of this organelle is disrupted due to various external causes or intracellular events, resulting to a buildup of misfolded or unfolded proteins. Concerns in this area are possible. Some illnesses, cell death, and metabolic abnormalities are examples. The cell's stress response mechanism is the unfolded protein response (UPR). Reduced translation, degradation of unfolded proteins to reduce damage, and increased production of cell-mate proteins all aid in the folding of nascent proteins. This research uses a literature review approach to learn about the ER, an experiment on ER Stress, the reaction mechanism of unfolded protein response (UPR), diseases induced by ER Stress, and the significance of UPR in these illnesses.