Interferon-induced upregulation and cytoplasmic localization of Myc-interacting protein Nmi.

Nmi interacts with c-Myc, N-Myc, Max, and fos, as demonstrated by yeast two-hybrid and coimmunoprecipitation assays. Nmi is partially homologous to IFP 35, an interferon (IFN)-inducible protein. In this study, we show that basal expression of Nmi is upregulated by IFN in multiple tumor-derived cell lines. Treatment with IFN results in an increased amount of cytoplasmic Nmi distributed in a punctate granular pattern. We also demonstrate that Nmi is expressed in various fetal and adult tissues. As Nmi does not contain a known DNA-binding motif, it has the potential to form inactive heterodimers with its putative DNA-binding partners. Our studies suggest that Nmi may modulate its binding partners in an IFN-inducible manner.