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Cooperation of Stat2 and p300/CBP in signalling induced by interferon-α

Nature volume 383, pages 344–347 (1996)Cite this article

Abstract

THE transcription factor ISGF3 transduces interferon (IFN)-α signals and activates the transcription of cellular antiviral defence genes1,2. Adenovirus E1A blocks the IFN-α response, allowing unhindered viral replication3–5. ISGF3 consists of Statl, Stat2 and p48. Here we show that p300 and/or CBP (CREB-binding protein), which are transcription adaptors targeted by E1A, interact specifically with Stat2. Binding occurs between the first cysteine–histidine-rich region of p300/CBP and the carboxy-terminal segment of Stat2, a domain essential for ISGF3 function6. We find that this domain of Stat2 has transactivation potential, which correlates with its binding to p300/CBP. Moreover, E1A represses Stat2 transactivation and IFN-α-activated transcription by inhibiting p300/CBP function. This provides a new mechanism for inhibition of the IFN-α-activated antiviral response by E1A, and supports the view that E1A binding to p300/CBP has functional significance for adenovirus replication in its natural host.

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Author notes

  1. Richard Eckner

    Present address: Institute for Molecular Biology, University of Zurich, CH-8057, Zurich, Switzerland

Authors and Affiliations

  1. Dana-Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts, 02115, USA

    Shoumo Bhattacharya, Richard Eckner, Steven Grossman, Elizabeth Oldread, Zoltan Arany, Alan D'Andrea & David M. Livingston

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  1. Shoumo Bhattacharya
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  2. Richard Eckner
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  3. Steven Grossman
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Bhattacharya, S., Eckner, R., Grossman, S. et al. Cooperation of Stat2 and p300/CBP in signalling induced by interferon-α. Nature 383, 344–347 (1996). https://doi.org/10.1038/383344a0

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