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    UFMylation of 14-3-3ε enhances RIG-I signaling by stabilizing downstream events, promoting interferon induction. This post-translational modification is crucial for innate antiviral defense.

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    Area of Science:

    • Immunology
    • Molecular Biology
    • Cellular Biology

    Background:

    • Post-translational modifications regulate key signaling pathways, including RIG-I signaling.
    • UFMylation (UFM1 conjugation) was previously shown to promote RIG-I signaling by enhancing RIG-I and 14-3-3ε interaction.

    Purpose of the Study:

    • To investigate the novel role of 14-3-3ε UFMylation in regulating RIG-I signaling.
    • To identify the specific sites and functional consequences of 14-3-3ε UFMylation.

    Main Methods:

    • Site-directed mutagenesis to create UFMylation-deficient 14-3-3ε mutants (K50R/K215R).
    • Analysis of interferon induction (Type I and III) in response to RIG-I activation.
    • Assessment of 14-3-3ε binding to RIG-I.

    Main Results:

    • UFMylation of 14-3-3ε occurs at lysine residues K50 and K215, resulting in mono-UFMylation.
    • Mutating K50 and K215 to arginine abolished 14-3-3ε UFMylation and impaired interferon induction.
    • UFMylation of 14-3-3ε enhanced downstream signaling without affecting its direct interaction with RIG-I.

    Conclusions:

    • UFMylation of 14-3-3ε is a novel regulatory mechanism that promotes RIG-I signaling and interferon production.
    • This modification stabilizes signaling events downstream of RIG-I activation, contributing to antiviral defense.
    • UFMylation of 14-3-3ε highlights its broader role in innate immunity and suggests potential therapeutic targets.