{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qi F"],"funding":["Fundamental Research Funds for the Central Universities","National Natural Science Foundation of China"],"pagination":["e22409"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12166272"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["36(8)"],"pubmed_abstract":["Interferon regulatory factor 7 (IRF7), as the interferon-stimulated gene, maximally drives type I interferon (IFN) production. However, the mechanisms by which the biological function of IRF7 is regulated remain elusive. In this study, we found that IRF7 selectively interacted with the neuralized E3 ubiquitin-protein ligase 3 (NEURL3). In concomitant with IRF7 induction, NEURL3 is upregulated by NF-κB signaling in the late phase of viral infection. Moreover, NEURL3 augmented the host antiviral immune response through ubiquitinating IRF7. A mechanistic study revealed that NEURL3 triggered K63-linked poly-ubiquitination on IRF7 lysine 375, which in turn epigenetically enhanced the transcription of interferon-stimulated genes (ISGs) through disruption of the association of IRF7 with Histone D"],"journal":["FASEB journal : official publication of the Federation of American Societies for Experimental Biology"],"pubmed_title":["E3 ubiquitin ligase NEURL3 promotes innate antiviral response through catalyzing K63-linked ubiquitination of IRF7."],"pmcid":["PMC12166272"],"funding_grant_id":["81991505","82022032","BMU2018YJ003","82171826"],"pubmed_authors":["Luo J","Zhang X","Qi F","Lu D","Ren C","Wang L","Zhao X"],"additional_accession":[]},"is_claimable":false,"name":"E3 ubiquitin ligase NEURL3 promotes innate antiviral response through catalyzing K63-linked ubiquitination of IRF7.","description":"Interferon regulatory factor 7 (IRF7), as the interferon-stimulated gene, maximally drives type I interferon (IFN) production. However, the mechanisms by which the biological function of IRF7 is regulated remain elusive. In this study, we found that IRF7 selectively interacted with the neuralized E3 ubiquitin-protein ligase 3 (NEURL3). In concomitant with IRF7 induction, NEURL3 is upregulated by NF-κB signaling in the late phase of viral infection. Moreover, NEURL3 augmented the host antiviral immune response through ubiquitinating IRF7. A mechanistic study revealed that NEURL3 triggered K63-linked poly-ubiquitination on IRF7 lysine 375, which in turn epigenetically enhanced the transcription of interferon-stimulated genes (ISGs) through disruption of the association of IRF7 with Histone D","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-07-26T03:07:25.728Z","creation":"2025-07-26T03:07:25.728Z"},"accession":"S-EPMC12166272","cross_references":{"pubmed":["35792897"],"doi":["10.1096/fj.202200316R"]}}