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Updated: May 5, 2026

High-throughput Quantitative Real-time RT-PCR Assay for Determining Expression Profiles of Types I and III Interferon Subtypes
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Published on: March 24, 2015

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Acetylation-dependent signal transduction for type I interferon receptor

Xiaoli Tang1, Jin-Song Gao, Ying-jie Guan

  • 1Department of Surgery, Brown University Medical School, Rhode Island Hospital, 593 Eddy Street, Providence, RI 02903, USA.

Cell
|October 10, 2007
PubMed

Insights

Cytokine receptor signaling involves acetylation. CREB-binding protein (CBP) acetylates interferon alpha receptor 2 (IFNAR2), enabling antiviral gene regulation via the ISGF3 complex.

Area of Science:

  • Cellular signaling
  • Molecular biology
  • Immunology

Background:

  • Cytokine-activated receptors initiate signaling by recruiting kinases.
  • Phosphorylation of receptors enables docking of SH2 domain-bearing factors.

Purpose of the Study:

  • To investigate the role of CREB-binding protein (CBP) in type 1 interferon (IFNα) signaling.
  • To elucidate the mechanism of interferon regulatory factor 9 (IRF9) recruitment and ISGF3 complex formation.

Main Methods:

  • Co-immunoprecipitation assays to study protein interactions.
  • In vitro acetylation assays to determine CBP activity.
  • Site-directed mutagenesis to identify critical residues.

Main Results:

  • IFNα receptors recruit cytoplasmic CBP upon IFNα stimulation.
  • CBP acetylates IFNAR2 on Lys399, creating a docking site for IRF9.
  • Acetylation of IRF9 and STAT2 within their DNA-binding domains is crucial for ISGF3 complex activation and antiviral gene expression.

Conclusions:

  • Acetylation, mediated by CBP, is a critical regulatory mechanism in cytokine receptor signal transduction.
  • This pathway highlights a novel role for acetylation in antiviral immunity.

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