Modulators of Endoplasmic Reticulum Stress 2016

Dear Colleagues,

The accumulation of unfolded proteins in the lumen of endoplasmic reticulum (ER) causes ER stress and induces the unfolded protein response (UPR). The UPR alleviates stress by inhibiting protein synthesis, and by promoting the expression of molecular chaperones and other factors involved in ER-associated protein degradation (ERAD). Under cellular stress, the ER activates three branches of the UPR: (i) the protein kinase RNA-activated-like ER kinase–eukaryotic translation initiation factor 2 alpha (PERK-eIF2α) pathway, (ii) the inositol-requiring enzyme 1–X-box binding protein 1 (IRE1-XBP1) pathway, and (iii) the activating transcription factor 6 (ATF6) pathway. However, if ER stress is prolonged and severe, the UPR can result in cell death through the activation of apoptotic pathways. Accumulating evidence indicates that the ER stress is involved in the pathogenesis of not only the protein misfolding disorders such as neurodegenerative disease, but also in the cytotoxicity of drugs, environmental pollutants, and industrial chemicals. Thus, the determination of the modulators that activate or inhibit ER stress signaling pathways is an important field of research. The articles in this special issue will address research aspects related to the inducers or modulators of ER stress in the biological, toxicological, and medical fields.

Prof. Dr. Masato Matsuoka
Guest Editor

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