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Biochem Biophys Res Commun. 2006 Dec 15;351(2):540-6. Epub 2006 Oct 18.

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

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Division of Gene Regulation and Signal Transduction, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Japan.


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.

[Indexed for MEDLINE]

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