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.
Department of Pediatrics, Stanford Medical Center, CA 94305, USA.
S J
SJ
Lebrun
R L
RL
Shpall
L
L
Naumovski
D002352:Carrier Proteins / Q000032:analysis / Q000096:biosynthesis*; D002460:Cell Line; D003593:Cytoplasm / Q000378:metabolism*; D006801:Humans; D016898:Interferon-alpha / Q000494:pharmacology*; D047908:Intracellular Signaling Peptides and Proteins; D011485:Protein Binding; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism; D015854:Up-Regulation
D002352:Carrier Proteins; D016898:Interferon-alpha; D047908:Intracellular Signaling Peptides and Proteins; C099927:NMI protein, human; D016271:Proto-Oncogene Proteins c-myc