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- W2782852914 abstract "Abstract Transactivation response element RNA-binding protein (TRBP or TARBP2) initially identified to play an important role in human immunodeficiency virus (HIV) replication also has emerged as a regulator of microRNA biogenesis. In addition, TRBP functions in signaling pathways by negatively regulating the interferon-induced double-stranded RNA (dsRNA)-activated protein kinase (PKR) during viral infections and cell stress. During cellular stress, PKR is activated and phosphorylates the α subunit of the eukaryotic translation factor eIF2, leading to the cessation of general protein synthesis. TRBP inhibits PKR activity by direct interaction as well as by binding to PKR’s two known activators, dsRNA and PACT, thus preventing their interaction with PKR. In this study, we demonstrate for the first time that TRBP is phosphorylated in response to oxidative stress and upon phosphorylation, inhibits PKR more efficiently promoting cell survival. These results establish that PKR regulation through stress-induced TRBP phosphorylation is an important mechanism ensuring cellular recovery and preventing apoptosis due to sustained PKR activation." @default.
- W2782852914 created "2018-01-26" @default.
- W2782852914 creator A5028524295 @default.
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- W2782852914 date "2018-01-18" @default.
- W2782852914 modified "2023-10-16" @default.
- W2782852914 title "Stress-induced TRBP phosphorylation enhances its interaction with PKR to regulate cellular survival" @default.
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- W2782852914 doi "https://doi.org/10.1038/s41598-018-19360-8" @default.
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