PSMD13 inhibits NF-κB pathway by targeting TAK1 for K63-linked ubiquitination in miiuy croaker (Miichthys miiuy)

Qi Li1, Ya Chen1, Pengfei Wang1

  • 1Laboratory of Fish Molecular Immunology, College of Fisheries and Life Science, Shanghai Ocean University, Shanghai, China.

PubMed

Insights

Proteasome 26S subunit, non-ATPase (PSMD) 13 regulates innate immunity by inhibiting the NF-κB pathway. PSMD13 targets transforming growth factor-β activated kinase 1 (TAK1), reducing its ubiquitination and expression.

Area of Science:

  • Innate immunity
  • Molecular biology
  • Cellular signaling

Background:

  • Transforming growth factor-β activated kinase 1 (TAK1) is crucial in Toll-like receptor (TLR)-mediated NF-κB signaling.
  • The role of Proteasome 26S subunit, non-ATPase (PSMD) 13 in innate immune regulation remains largely unknown.

Purpose of the Study:

  • To elucidate the mechanism by which PSMD13 regulates innate immunity.
  • To investigate the interaction between PSMD13 and the NF-κB pathway.

Main Methods:

  • Analyzing PSMD13 mRNA expression levels following Vibrio harveyi stimulation.
  • Investigating the effect of PSMD13 on TAK1 ubiquitination and NF-κB pathway activity.

Main Results:

  • PSMD13 mRNA expression significantly increased upon Vibrio harveyi challenge.
  • PSMD13 was found to inhibit the NF-κB pathway by targeting TAK1.
  • PSMD13 significantly reduced K63-linked ubiquitination of TAK1, thereby inhibiting its expression.

Conclusions:

  • PSMD13 plays a regulatory role in innate immunity by inhibiting the TAK1-mediated NF-κB pathway.
  • This study expands understanding of PSMD family functions in immune responses.
  • Provides novel insights into mammalian innate immune regulation mechanisms.

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