GlutaredoxinV1, Main, Exploration, bibRecord, 000A25

Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling.

Identifieur interne : 000A25 ( Main/Exploration ); précédent : 000A24; suivant : 000A26

Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling.

Auteurs : Eleni Chantzoura [Grèce] ; Efthimios Prinarakis ; Dimitris Panagopoulos ; George Mosialos ; Giannis Spyrou

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2010.

RBID : pubmed:21078302

Descripteurs français

English descriptors

KwdEn :
- Glutaredoxins (metabolism), Glutathione (metabolism), HEK293 Cells (MeSH), HeLa Cells (MeSH), Humans (MeSH), NF-kappa B (metabolism), Protein Processing, Post-Translational (MeSH), RING Finger Domains (MeSH), Receptors, Interleukin-1 (metabolism), Signal Transduction (MeSH), TNF Receptor-Associated Factor 6 (metabolism), Toll-Like Receptor 4 (metabolism), Ubiquitination (MeSH).
MESH :
- chemical , metabolism : Glutaredoxins, Glutathione, NF-kappa B, Receptors, Interleukin-1, TNF Receptor-Associated Factor 6, Toll-Like Receptor 4.
- HEK293 Cells, HeLa Cells, Humans, Protein Processing, Post-Translational, RING Finger Domains, Signal Transduction, Ubiquitination.

Abstract

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.

DOI: 10.1016/j.bbrc.2010.11.029
PubMed: 21078302

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Glutaredoxins (metabolism)</term>
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<term>HeLa Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>NF-kappa B (metabolism)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>RING Finger Domains (MeSH)</term>
<term>Receptors, Interleukin-1 (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>TNF Receptor-Associated Factor 6 (metabolism)</term>
<term>Toll-Like Receptor 4 (metabolism)</term>
<term>Ubiquitination (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HEK293 (MeSH)</term>
<term>Cellules HeLa (MeSH)</term>
<term>Domaines à doigts de zinc de type RING (MeSH)</term>
<term>Facteur de transcription NF-kappa B (métabolisme)</term>
<term>Facteur-6 associé aux récepteurs de TNF (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Récepteur de type Toll-4 (métabolisme)</term>
<term>Récepteurs à l'interleukine-1 (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
<term>Ubiquitination (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
<term>NF-kappa B</term>
<term>Receptors, Interleukin-1</term>
<term>TNF Receptor-Associated Factor 6</term>
<term>Toll-Like Receptor 4</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur de transcription NF-kappa B</term>
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<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Récepteur de type Toll-4</term>
<term>Récepteurs à l'interleukine-1</term>
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<term>HeLa Cells</term>
<term>Humans</term>
<term>Protein Processing, Post-Translational</term>
<term>RING Finger Domains</term>
<term>Signal Transduction</term>
<term>Ubiquitination</term>
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<term>Cellules HeLa</term>
<term>Domaines à doigts de zinc de type RING</term>
<term>Humains</term>
<term>Maturation post-traductionnelle des protéines</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>Copyright © 2010 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
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<ForeName>Giannis</ForeName>
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Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling.

Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling.

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Abstract

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