Two contact regions between Stat1 and CBP/p300 in interferon gamma signaling.

Interferon gamma (IFN-gamma) induces rapid tyrosine phosphorylation of the latent cytoplasmic transcription factor, Stat1, which then forms homodimers, translocates to the nucleus and participates in IFN-gamma-induced transcription. However, little is known of the interactions between Stat1 and the general transcription machinery during transcriptional activation. We show here that Stat1 can ...
directly interact with the CREB-binding protein (CBP)/p300 family of transcriptional coactivators. Specifically, two interaction regions were identified: the amino-terminal region of Stat1 interacts with the CREB-binding domain of CBP/p300 and the carboxyl-terminal region of Stat1 interacts with the domain of CBP/p300 that binds adenovirus E1A protein. Transfection experiments suggest a role for these interactions in IFN-gamma-induced transcription. Because CBP/p300-binding is required for the adenovirus E1A protein to regulate transcription of many genes during viral replication and cellular transformation, it is possible that the anti-viral effect of IFN-gamma is based at least in part on direct competition by nuclear Stat1 with E1A for CBP/p300 binding.
Mesh Terms:
Adenovirus E1A Proteins, Animals, CREB-Binding Protein, Cell Line, DNA-Binding Proteins, Glutathione Transferase, Humans, Interferon-gamma, Nuclear Proteins, Osteosarcoma, Phosphorylation, Recombinant Fusion Proteins, STAT1 Transcription Factor, Signal Transduction, Trans-Activators, Transcription Factors, Transcription, Genetic, Transcriptional Activation, Transfection
Proc. Natl. Acad. Sci. U.S.A.
Date: Dec. 24, 1996
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