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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
Glycogen synthase kinase 3β ubiquitination by TRAF6 regulates TLR3-mediated pro-inflammatory cytokine production
Ryeojin Ko1, Jin Hee Park1, Hyunil Ha2
1Department of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul 120-750, South Korea.
Abstract:
TRAF6 is critical for the production of inflammatory cytokines in various TLR-mediated signalling pathways. However, it is poorly understood how TRAF6 regulates TLR3 responses. Here we demonstrate that GSK3β interacts with TRAF6 and positively regulates the TLR3-mediated signalling. Suppression of GSK3β expression or its kinase activity drastically reduces the production of inflammatory cytokines and the induction of c-Fos by decreasing ERK and p38 phosphorylation. GSK3β physically associates with TRAF6 in a TLR3 ligand poly I:C-dependent manner. TRAF6 is determined to be a direct E3 ligase for GSK3β, and TRAF6-mediated GSK3β ubiquitination is essential for poly I:C-dependent cytokine production by promoting the TLR3 adaptor protein TRIF-assembled signalling complex.
Insights
Glycogen synthase kinase 3 beta (GSK3β) positively regulates Toll-like receptor 3 (TLR3) signaling. TRAF6 ubiquitination of GSK3β is essential for inflammatory cytokine production via the TRIF complex.
Area of Science:
- Immunology
- Molecular Biology
- Cell Signaling
Background:
- Toll-like receptor 3 (TLR3) pathways are crucial for innate immunity.
- Tumor necrosis factor receptor-associated factor 6 (TRAF6) is vital for inflammatory cytokine production.
- The precise role of TRAF6 in TLR3 signaling remains unclear.
Purpose of the Study:
- To elucidate the mechanism by which TRAF6 regulates TLR3-mediated signaling.
- To investigate the interaction between TRAF6 and Glycogen synthase kinase 3 beta (GSK3β) in TLR3 responses.
Main Methods:
- Co-immunoprecipitation assays to detect protein interactions.
- Western blotting to assess protein phosphorylation and ubiquitination.
- Quantitative real-time PCR to measure cytokine production.
- Gene silencing and kinase inhibition to study protein function.
Main Results:
- GSK3β interacts with TRAF6 and enhances TLR3 signaling.
- GSK3β suppression reduces inflammatory cytokine production and c-Fos induction by decreasing ERK and p38 phosphorylation.
- TRAF6 directly ubiquitinates GSK3β in a poly I:C-dependent manner.
- TRAF6-mediated GSK3β ubiquitination is critical for assembling the TRIF-containing signaling complex.
Conclusions:
- GSK3β acts as a positive regulator of TLR3 signaling.
- TRAF6-mediated ubiquitination of GSK3β is a key step in TLR3-induced inflammatory cytokine production.
- This study reveals a novel regulatory mechanism in TLR3 innate immune responses.
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