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- W4387605468 abstract "RNase L is a regulated endoribonuclease in higher vertebrates that functions in antiviral innate immunity. Interferons induce OAS enzymes that sense double-stranded RNA of viral origin leading to synthesis of 2-prime,5-prime-oligoadenylate (2-5A) activators of RNase L. However, it is unknown precisely how RNase L inhibits viral infections. To isolate effects of RNase L from other effects of double-stranded RNA or virus, 2-5A was directly introduced into cells. Here we report that RNase L activation by 2-5A causes a ribotoxic stress response that requires the ribosome-associated MAP3K, ZAKa. Subsequently, the stress-activated protein kinases (SAPK) JNK and p38a; are phosphorylated. RNase L activation profoundly altered the transcriptome by widespread depletion of mRNAs associated with different cellular functions, but also by SAPK-dependent induction of inflammatory genes. Our findings show that 2-5A is a ribotoxic stressor that causes RNA damage through RNase L triggering a ZAKa; kinase cascade leading to proinflammatory signaling and apoptosis." @default.
- W4387605468 created "2023-10-14" @default.
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- W4387605468 date "2023-10-12" @default.
- W4387605468 modified "2023-10-14" @default.
- W4387605468 title "Initiation of a ZAKa-dependent Ribotoxic Stress Response by the Innate Immunity Endoribonuclease RNase L" @default.
- W4387605468 doi "https://doi.org/10.1101/2023.10.12.562082" @default.
- W4387605468 hasPublicationYear "2023" @default.
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