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Related Experiment Video

Updated: Jul 10, 2025

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
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RNF138 Downregulates Antiviral Innate Immunity by Inhibiting IRF3 Activation.

Xianhuang Zeng1, Chaozhi Liu2, Jinhao Fan3

  • 1Taikang Medical School (School of Basic Medical Sciences), Wuhan University, Wuhan 430071, China.

International Journal of Molecular Sciences
|November 25, 2023
PubMed
Summary
This summary is machine-generated.

RNF138 negatively regulates antiviral responses by inhibiting IRF3 activation. This E3 ligase targets PTEN, blocking IRF3 nuclear import and type I interferon production during viral infections.

Keywords:
IRF3PTENRNF138antiviral natural immunity

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Area of Science:

  • Immunology
  • Molecular Biology
  • Virology

Background:

  • Viral infections trigger type I interferons (IFNs) via IRF3 and NF-κB transcription factors.
  • Cellular antiviral responses are crucial for host defense against viral pathogens.

Purpose of the Study:

  • To identify novel negative regulators of virus-triggered IRF3 activation and type I IFN induction.
  • To elucidate the molecular mechanism by which RNF138 modulates antiviral signaling.

Main Methods:

  • Overexpression and knockout studies of RNF138 in cellular models.
  • Analysis of IRF3 activation, IFNB1 gene transcription, and PTEN ubiquitination.
  • Investigation of protein-protein interactions between PTEN and IRF3.

Main Results:

  • RNF138 overexpression inhibited virus-induced IRF3 activation and IFNB1 transcription.
  • RNF138 knockout enhanced virus-induced IRF3 activation and IFNB1 transcription.
  • RNF138 promotes PTEN ubiquitination, inhibiting PTEN-IRF3 interaction and IRF3 nuclear translocation.

Conclusions:

  • RNF138 acts as a negative regulator of antiviral signaling pathways.
  • RNF138 inhibits IRF3 nuclear import by modulating PTEN interactions.
  • These findings offer new insights into the molecular mechanisms governing cellular antiviral immunity.