IndraLab

Statements


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"USP3 was reported to deubiquitinate RIG-1-like receptors, and inhibits type I interferon signaling [10] ."

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"USP3 specifically negatively regulates type I IFN signaling by removal of the K63-linked polyubiquitin chains from RIG-I ( Cui et al., 2014 )."

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"USP3 negatively regulates the activation of type 1 interferon (IFN-I) signaling by specifically targeting Retinoic acid-inducible gene I lysine 63(RIG-I K63)-linked polyubiquitin chains and removing them, resulting in IFN-I inhibition."

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"USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors."

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"For example, USP3 and CYLD were reported to negatively regulate type I IFN induction by targeting RIG-I ( Cui et al., 2014 ; Friedman et al., 2008 ); OTUD1 potently inhibits innate antiviral immunity [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"However, the ZnF domain of USP3 alone cannot inhibit RIG-I-induced type I IFN activation, and the UCH domain may require ZnF for maximal catalytic activity, suggesting that both intact ZnF and the catalytic domain are required for USP3 to exert its deubiquitination function [11]."

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"USP3 also negatively regulates IFN signaling by interacting with RIG-I and MDA5, but not with other downstream signaling proteins like MAVS, TBK1, IKKi, IRF3, TRAF3, or TRAF6."