Abstract 1548 PKR activation in response to endoplasmic reticulum (ER) stress

Disruption of endoplasmic reticulum (ER) homeostasis is sensed by the ER resident protein kinase, PERK. PERK phosphorylates the a subunit of the eukaryotic translation initiation factor 2 (eIF2α), which prevents translation initiation, leading to a decrease in general protein synthesis while allowing induction of selected genes (e. g. ATF4) to promote cellular recovery. PKR is another protein kinase that phosphorylates eIF2a, however, it is normally activated by double-stranded RNA present during viral infections.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.110097
Primary Topic
Endoplasmic Reticulum Stress and Disease
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 1548 PKR activation in response to endoplasmic reticulum (ER) stress

Rekha C. Patel, Emily Swager, Sanjana B. Parise
Journal of Biological Chemistry
Endoplasmic Reticulum Stress and Disease
article

Abstract 1548 PKR activation in response to endoplasmic reticulum (ER) stress

Rekha C. Patel, Emily Swager, Sanjana B. Parise
article en

Abstract

Disruption of endoplasmic reticulum (ER) homeostasis is sensed by the ER resident protein kinase, PERK. PERK phosphorylates the a subunit of the eukaryotic translation initiation factor 2 (eIF2α), which prevents translation initiation, leading to a decrease in general protein synthesis while allowing induction of selected genes (e. g. ATF4) to promote cellular recovery. PKR is another protein kinase that phosphorylates eIF2a, however, it is normally activated by double-stranded RNA present during viral infections.

Journal of Biological ChemistryVol. 301(5)
South Carolina State University (US), University of South Carolina (US)
U.S. Department of Defense, National Institutes of Health
Zero hunger
Openalex Percentile: Top 86%
Endoplasmic Reticulum Stress and Disease
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