Two Contact Regions between Stat1 and CBP/p300 in Interferon γ Signaling

Interferon γ (IFN-γ ) induces rapid tyrosine phosphorylation of the latent cytoplasmic transcription factor, Stat1, which then forms homodimers, translocates to the nucleus and participates in IFN-γ -induced transcription. However, little is known of the interactions between Stat1 and the general tr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1996-12, Vol.93 (26), p.15092-15096
Main Authors: Zhang, Jue J., Vinkemeier, Uwe, Gu, Wei, Chakravarti, Debabrata, Horvath, Curt M., Darnell, James E.
Format: Article
Language:English
Subjects:
adenovirus
Adenovirus E1A Proteins - metabolism
Animals
Antibodies
Biological Sciences
Cell Line
Cell lines
Cell nucleus
CREB-Binding Protein
DNA
DNA-Binding Proteins - metabolism
Genes
Glutathione Transferase - biosynthesis
Humans
Interferon-gamma - pharmacology
Interferons
Nuclear Proteins - metabolism
Osteosarcoma
Phosphorylation
Proteins
Recombinant Fusion Proteins - metabolism
Signal Transduction
STAT1 Transcription Factor
Trans-Activators - metabolism
Transcription Factors - metabolism
Transcription, Genetic - drug effects
Transcriptional Activation
Transfection
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Summary:Interferon γ (IFN-γ ) induces rapid tyrosine phosphorylation of the latent cytoplasmic transcription factor, Stat1, which then forms homodimers, translocates to the nucleus and participates in IFN-γ -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 carboxylterminal 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-γ -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-γ is based at least in part on direct competition by nuclear Stat1 with E1A for CBP/p300 binding.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.93.26.15092