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FIGURE 1. From: The role of endoplasmic reticulum stress and the unfolded protein response in fibrosis.

Signaling pathways of the UPR. Accumulation of unfolded proteins in ER lumen results in the ER stress. In response to ER stress, BiP dissociates from the ER stress transducers and binds to unfolded and misfolded proteins, resulting in the activation of the ER stress transducers: PERK, IRE1, and ATF6. Activation of PERK increases phosphorylation of eIF2α, leading to attenuation of protein synthesis and an increase in ATF4 translation. During prolonged stress, ATF4 can induce CHOP, a proapoptotic transcription factor. Once activated, IRE1 splices XBP1 producing the active form XBP1-S (spliced XBP1), which upregulates ER chaperones and proteins implicated in the ER-associated protein degradation (ERAD). ATF6 translocates to Golgi, in which it is activated by proteolysis. Activated ATF6 transcriptionally induces ERAD genes and upregulates CHOP expression. ER, endoplasmic reticulum; UPR, unfolded protein response.

Stefania Lenna, et al. Curr Opin Rheumatol. 2012 November;24(6):10.1097/BOR.0b013e3283588dbb.

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