Endoplasmic Reticulum Stress Signaling Pathway: From Bench to Bedside

Dear Colleagues,

The endoplasmic reticulum (ER) is the largest membrane organelle found in all eukaryotes and plays a central role in the oxidative folding of the majority of secretory and membrane proteins. To facilitate protein folding, the ER utilizes a number of folding enzymes and molecular chaperones, as well as oxidoreductases, which drive the formation of disulfide bonds to maintain stable protein structure. When the demand for protein folding exceeds the ER folding capacity, unfolded/misfolded proteins accumulate in the ER, leading to the activation of a signal transduction pathway known as the Unfolded Protein Response (UPR). The mammalian UPR consists of three branches (IRE1, PERK, and ATF6) that restore ER homeostasis by inhibiting protein synthesis, enhancing expression of folding enzymes and chaperones, and promoting clearance of non-native proteins. Physiologically, the balance between ER stress and the UPR is critical to maintaining healthy cell and tissue functions. However, prolonged ER stress and UPR activation can be maladaptive and ultimately lead to cellular dysfunction and death. Thus, in recent years, ER stress and the UPR have emerged as targets for drug development for major human diseases, including diabetes, cancer, infection, and neurodegenerative disorders.

This Special Issue seeks to unveil the molecular mechanisms through which cells respond to counter ER stress, explore the involvement of ER stress in the progression of diseases, and identify novel targets or molecules within the ER stress signaling pathway to treat human diseases.

Dr. Samuel Stephens
Dr. Jianchao Zhang
Guest Editors

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• ER stress
• oxidative protein folding
• ER redox
• ER calcium homeostasis
• UPR
• diabetes
• cancer
• virus