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[Endoplasmic reticulum-mediated integrated stress response].

Tian-Qi Tao1, Xiu-Hua Liu

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Summary
This summary is machine-generated.

The integrated stress response (ISR), regulated by protein kinase R-like ER kinase (PERK), is a conserved cellular defense against stress. This review covers ISR

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Stress Response

Background:

  • The integrated stress response (ISR) is a conserved cellular mechanism activated by various stressors like oxidative damage, amino acid deficiency, and endoplasmic reticulum (ER) stress.
  • The eukaryotic translation initiator factor 2alpha (eIF2alpha) pathway is central to ISR.
  • Protein kinase R-like ER kinase (PERK) is identified as a key upstream regulator within the ISR pathway.

Purpose of the Study:

  • To review the factors that induce the integrated stress response (ISR).
  • To elucidate the signaling pathways involved in ISR, particularly those mediated by the endoplasmic reticulum (ER).
  • To summarize the physiological and pathophysiological roles of ER-mediated ISR.

Main Methods:

  • Literature review of ISR and ER stress signaling pathways.
  • Analysis of the role of PERK, inositol-requiring enzyme-1 (IRE1), and activating transcription factor 6 (ATF6) in ISR.
  • Synthesis of information on factors inducing ISR and its downstream effects.

Main Results:

  • ISR is triggered by diverse cellular stresses, with PERK playing a pivotal role upstream of eIF2alpha.
  • PERK integrates stress signals by modulating protein synthesis, folding, autophagy, and apoptosis.
  • PERK interacts with IRE1 and ATF6 signaling pathways, highlighting complex cross-talk in ER stress response.

Conclusions:

  • The endoplasmic reticulum-mediated integrated stress response is a critical adaptive mechanism.
  • Understanding ISR pathways, particularly PERK signaling, is crucial for comprehending cellular responses to stress.
  • Dysregulation of ER-mediated ISR may contribute to various pathophysiological conditions.