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A ubiquitin E3 ligase Efp is up-regulated by interferons and conjugated with ISG15.

Nakasato N., Ikeda K., Urano T., Horie-Inoue K., Takeda S., Inoue S.

Interferon (IFN) regulates various target genes that mediate important roles in immune responses such as antiviral state. Protein ISG15-conjugation (ISGylation) is implicated in the IFN-induced antiviral response. Here we demonstrate that Efp mRNA as well as protein expression could be up-regulated by Type I IFN in HeLa cells and HepG2 cells. Luciferase assay reveals that the first intron of Efp gene contains a functional interferon-stimulated response element (ISRE) and electrophoretic mobility shift assay shows that the ISRE binds to signal transducer and activator of transcription 1 (STAT1). Chromatin immunoprecipitation assays have shown that the ISRE recruits STAT1 in vivo IFN-dependently. Moreover, we demonstrate that Efp protein could be conjugated with not only ubiquitin but also ISG15. These data suggest that Efp is an IFN-responsive gene that potentially mediates IFN actions, involved in ISGylation and ubiquitination of proteins including Efp itself.

Biochem. Biophys. Res. Commun. 351:540-546(2006) [PubMed] [Europe PMC]

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