Functional association of Nmi with Stat5 and Stat1 in IL-2- and IFNgamma-mediated signaling.
Using the coiled-coil region of Stat5b as the bait in a yeast two-hybrid screen, we identified the association of Nmi, a protein of unknown function previously reported as an N-Myc interactor. We further show that Nmi interacts with all STATs except Stat2. We evaluated two cytokine systems, IL-2 and IFNgamma, ... and demonstrate that Nmi augments STAT-mediated transcription in response to these cytokines. Interestingly, Nmi lacks an intrinsic transcriptional activation domain; instead, Nmi enhances the association of CBP/p300 coactivator proteins with Stat1 and Stat5, and together with CBP/p300 can augment IL-2- and IFNgamma-dependent transcription. Therefore, our data not only reveal that Nmi can potentiate STAT-dependent transcription, but also suggest that it can augment coactivator protein recruitment to at least some members of a group of sequence-specific transcription factors.
Mesh Terms:
CREB-Binding Protein, Carrier Proteins, Cell Line, Transformed, Cells, Cultured, DNA-Binding Proteins, Humans, Interferon-gamma, Interleukin-2, Intracellular Signaling Peptides and Proteins, Lymphocytes, Milk Proteins, Nuclear Proteins, Recombinant Fusion Proteins, STAT1 Transcription Factor, STAT2 Transcription Factor, STAT5 Transcription Factor, Signal Transduction, Trans-Activators, Transcription, Genetic
CREB-Binding Protein, Carrier Proteins, Cell Line, Transformed, Cells, Cultured, DNA-Binding Proteins, Humans, Interferon-gamma, Interleukin-2, Intracellular Signaling Peptides and Proteins, Lymphocytes, Milk Proteins, Nuclear Proteins, Recombinant Fusion Proteins, STAT1 Transcription Factor, STAT2 Transcription Factor, STAT5 Transcription Factor, Signal Transduction, Trans-Activators, Transcription, Genetic
Cell
Date: Jan. 08, 1999
PubMed ID: 9989503
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