G3BP1 methylation by PRMT5 facilitates its recruitment of TBK1 for IRF3 activation during host response to foreign ribonucleic acids - Report - MDSpire

G3BP1 methylation by PRMT5 facilitates its recruitment of TBK1 for IRF3 activation during host response to foreign ribonucleic acids

  • By

  • Wen Song

  • Susana Soo-Yeon Kim

  • Candice Yam

  • Joey Teo

  • Jyue Yuan Lim

  • Xuezhi Bi

  • Hong-Hwa Lim

  • Kong-Peng Lam

  • July 8, 2026

  • 0 min

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Methylation of G3BP1 by PRMT5 Promotes TBK1 Recruitment for IRF3 Activation

Overview

This study identifies G3BP1 as a critical scaffold in innate immune signaling, facilitating TBK1 recruitment and IRF3 activation in response to extracellular RNA. G3BP1's arginine methylation by PRMT5 is essential for its interaction with TBK1 and subsequent interferon production.

Background

G3BP1 plays a significant role in the innate immune response by binding to key signaling molecules involved in the production of type I interferon. Understanding the mechanisms of G3BP1 in antiviral signaling is crucial, as dysregulation of this pathway can lead to inadequate immune responses during viral infections.

Data Highlights

No numerical data available in the source material.

Key Findings

  • G3BP1 binds to TBK1 and IRF3, essential for IFN-β production.
  • Knockdown of G3BP1 reduces TBK1-IRF3 complex formation and affects IRF3 phosphorylation.
  • G3BP1 constitutively associates with IRF3 and recruits TBK1 upon stimulation.
  • The C-terminal RGG region of G3BP1 is critical for binding IRF3 and TBK1.
  • Arginine methylation of G3BP1 by PRMT5 is necessary for its interaction with TBK1.

Clinical Implications

The findings highlight the importance of G3BP1 in the antiviral immune response.

Conclusion

G3BP1 serves as a signaling hub that facilitates TBK1 recruitment and IRF3 activation through arginine methylation by PRMT5.

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