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• W3100205438 abstract "Summary Viperin is a radical S-adenosylmethionine (SAM) enzyme that plays a multifaceted role in the cellular antiviral response. Viperin was recently shown to catalyze the SAM-dependent formation of 3′-deoxy-3′,4′-didehydro-CTP (ddhCTP), which inhibits some viral RNA polymerases. Viperin is also implicated in regulating K63-linked poly-ubiquitination of interleukin-1 receptor-associated kinase-1 (IRAK1) by the E3 ubiquitin ligase TNF Receptor-Associated Factor 6 (TRAF6) as part of the Toll-like receptor-7 and 9 (TLR7/9) innate immune signaling pathways. We show that IRAK1 and TRAF6 activate viperin to efficiently catalyze the radical-mediated dehydration of CTP to ddhCTP. Furthermore, poly-ubiquitination of IRAK1 requires the association of viperin with IRAK1 and TRAF6. Poly-ubiquitination appears dependent on structural changes induced by SAM binding to viperin but does not require catalytically active viperin. The synergistic activation of viperin and IRAK1 provides a mechanism that couples innate immune signaling with the production of the antiviral nucleotide ddhCTP." @default.
• W3100205438 created "2020-11-23" @default.
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• W3100205438 date "2018-05-21" @default.
• W3100205438 modified "2023-09-23" @default.
• W3100205438 title "Interactions between Viperin, IRAK1 andTRAF6 couple innate immune signaling to antiviral ribonucleotide synthesis" @default.
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• W3100205438 doi "https://doi.org/10.1101/318840" @default.
• W3100205438 hasPublicationYear "2018" @default.
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