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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
Published on: March 24, 2015
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.
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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