PMC:7281546 / 48812-49827 JSONTXT

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{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7281546","sourcedb":"PMC","sourceid":"7281546","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7281546","text":"The multiple stages of CoV replication cycle are closely associated with cellular membrane compartments, especially the endoplasmic reticulum (ER). The shape and functions of ER can be influenced by different physiological states and environmental conditions. When protein synthesis amounts surpass the folding capacity, the accumulation of a large amount of unfolded proteins in the ER leads to ER stress. Consequently, cells manifest a corresponding biological reaction that is widely known as the unfolded protein response (UPR) [233]. Once the UPR is induced, it alleviates the problems by host protein translation inhibition (by the transducer PKR-like ER protein kinase (PERK)-induced phosphorylation of eIF2a), stimulating protein folding. If homeostasis cannot be re-established, apoptosis eventually is triggered. Indeed, the activation of UPR regulates a wide variety of signaling pathways, such as apoptosis, autophagy, mitogen-activated protein (MAP) kinase activation, and innate immune response 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