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Glutaredoxin-1 regu...
Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling
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- Chantzoura, Eleni (författare)
- Center of Basic Research I, Biochemistry Division, Biomedical Research Foundation, Academy of Athens, Greece
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- Prinarakis, Efthimios (författare)
- Center of Basic Research I, Biochemistry Division, Biomedical Research Foundation, Academy of Athens, Greece
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- Panagopoulos, Dimitris (författare)
- School of Biology, Aristotle University of Thessaloniki, Greece
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- Mosialos, George (författare)
- School of Biology, Aristotle University of Thessaloniki, Greece
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- Spyrou, Giannis (författare)
- Center of Basic Research I, Biochemistry Division, Biomedical Research Foundation, Academy of Athens, Greece
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(creator_code:org_t)
- Elsevier, 2010
- 2010
- Engelska.
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Ingår i: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier. - 0006-291X .- 1090-2104. ; 403:3-4, s. 335-339
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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- Glutaredoxin-1 (GRX-1) is a cytoplasmic enzyme that highly contributes to the antioxidant defense system. It catalyzes the reversible reduction of glutathione-protein mixed disulfides, a process called deglutathionylation. Here, we investigated the role of GRX-1 in the pathway triggered by interleukin-1/Toll-like receptor 4 (IL-1R/TLR4) by using RNA interference (RNAi) in HEK293 and HeLa cells. TNF receptor-associated factor 6 (TRAF6) is an intermediate signalling molecule involved in the signal transduction by members of the interleukin-1/Toll-like receptor (IL-1R/TLR) family. TRAF6 has an E3 ubiquitin ligase activity which depends on the integrity of an amino-terminal really interesting new gene (RING) finger motif. Upon receptor activation, TRAF6 undergoes K63-linked auto-polyubiquitination which mediates protein-protein interactions and signal propagation. Our data showed that IL-1R and TLR4-mediated NF-κB induction was severely reduced in GRX-1 knockdown cells. We found that the RING-finger motif of TRAF6 is S-glutathionylated under normal conditions. Moreover, upon IL-1 stimulation TRAF6 undergoes deglutathionylation catalyzed by GRX-1. The deglutathionylation of TRAF6 is essential for its auto-polyubiquitination and subsequent activation. Taken together, our findings reveal another signalling molecule affected by S-glutathionylation and uncover a crucial role for GRX-1 in the TRAF6-dependent activation of NF-κB by IL-1R/TLRs.
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