Abstract
The endoplasmic reticulum (ER) is the major organelle in the cell for protein folding and plays an important role in cellular functions. The unfolded protein response (UPR) is activated in response to misfolded or unfolded protein accumulation in the ER. However, the UPR successfully alleviates the ER stress. If UPR fails to restore ER homeostasis, apoptosis is induced. ER stress plays an important role in innate immune signaling in response to microorganisms. Dysregulation of UPR signaling contributes to the pathogenesis of a variety of infectious diseases. In this review, we summarize the contribution of ER stress to the innate immune response to invading microorganisms and its role in the pathogenesis of infectious diseases.
Highlights
Frontiers in ImmunologyThe endoplasmic reticulum (ER) is the major organelle in the cell for protein folding and plays an important role in cellular functions
The endoplasmic reticulum (ER) is crucial for maintaining cellular calcium homeostasis and for the production, processing, and transport of proteins and lipids [1]
Spliced X-box binding protein-1 (XBP-1) mRNA induced by activated IRE1α regulates the expression of numerous target genes including ER chaperones and ER-associated protein degradation (ERAD) components [6, 7]
Summary
The endoplasmic reticulum (ER) is the major organelle in the cell for protein folding and plays an important role in cellular functions. The unfolded protein response (UPR) is activated in response to misfolded or unfolded protein accumulation in the ER. The UPR successfully alleviates the ER stress. If UPR fails to restore ER homeostasis, apoptosis is induced. ER stress plays an important role in innate immune signaling in response to microorganisms. Dysregulation of UPR signaling contributes to the pathogenesis of a variety of infectious diseases. We summarize the contribution of ER stress to the innate immune response to invading microorganisms and its role in the pathogenesis of infectious diseases
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