Abstract
A NODding acquaintance with ER stress.
Highlights
Accumulation of unfolded or misfolded proteins in the lumen of the endoplasmatic reticulum (ER) results in ER stress and induces the unfolded protein response (UPR)
The Bäumler and Tsolis groups showed that cells and mice deficient in the TNF receptorassociated factor 2 (TRAF2)–NOD1/2–RIPK2 axis are deficient in inositol requiring kinase 1α (IRE1α)-induced IL-6 production.[1]
Deletion of NOD1/2 solely reduced signaling downstream of IRE1α, whereas signaling from activating transcription factor 6 (ATF6) and protein kinase-like ER kinase (PERK) was not affected. These results show the role of NOD1/2 in the IRE1α arm of the ER stress response and raise the possibility of therapeutic intervention via the NOD pathway to reduce ER stress-induced inflammatory responses
Summary
Accumulation of unfolded or misfolded proteins in the lumen of the endoplasmatic reticulum (ER) results in ER stress and induces the unfolded protein response (UPR). The UPR consists of distinct cellular processes, such as increased transcription of repair proteins and chaperones, cell death and the induction of an inflammatory response resulting in the expression of proinflammatory cytokines such as IL-6.
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