Ubiquitination network in the type I IFN‐induced antiviral signaling pathway

Abstract Type I IFN (IFN‐I) is the body's first line of defense against pathogen infection. IFN‐I can induce cellular antiviral responses and therefore plays a key role in driving antiviral innate and adaptive immunity. Canonical IFN‐I signaling activates the Janus kinase (JAK)/signal transducer and activator of transcription (STAT) pathway, which induces the expression of IFN‐stimulated genes and eventually establishes a complex antiviral state in the cells. Ubiquitin is a ubiquitous cellular molecule for protein modifications, and the ubiquitination modifications of protein have been recognized as one of the key modifications that regulate protein levels and/or signaling activation. Despite great advances in understanding the ubiquitination regulation of many signaling pathways, the mechanisms by which protein ubiquitination regulates IFN‐I‐induced antiviral signaling have not been explored until very recently. This review details the current understanding of the regulatory network of ubiquitination that critically controls the IFN‐I‐induced antiviral signaling pathway from three main levels, including IFN‐I receptors, IFN‐I‐induced cascade signals, and effector IFN‐stimulated genes.