Recruitment of the Interleukin-1 Receptor (IL-1RI)-Associated Kinase IRAK to the IL-1RI Is Redox Regulated
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G.-F. Böl
Abstract
Interleukin-1 signaling is initiated by recruitment of adapter proteins and kinases to the type I interleukin-1 receptor (IL-1RI). It is modulated by accompanying redox processes at various levels, such as (auto-) phosphorylation of the IL-1RIassociated kinase IRAK, the phosphorylation of IκB and translocation and transcriptional activity of NFκB. Here we demonstrate that the thiolmodifying agents diamide, menadione, and phenylarsine oxide (PAO) block the recruitment of IRAK to the receptor without inhibiting kinase activity in the immunoprecipitated IL-1RI complex in the human epithelial cell line ECV304 and the murine T cell line EL-4. Inhibition of IRAK receptor association by menadione is reversible in a GSH-dependent manner, while the PAO effect proved to be irreversible. Phospholipid hydroperoxide glutathione peroxidase attenuates inhibition by menadione. Recruitment correlates with the presence of thiol groups in IRAK that were available for IAIT-labeling. We conclude that recruitment of IRAK to the IL-1RI is redox regulated by the glutathione system, a reduced status being a prerequisite for an appropiate IL-1 response.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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Artikel in diesem Heft
- Glutathione, Related Enzymology, and Leopold Flohé
- 'Lest I Forget Thee, Glutathione...'
- Glutathione Pathways in the Brain
- The Role of Glutathione Peroxidases in Trypanosomatids
- Cytoprotection against Oxidative Stress and the Regulation of Glutathione Synthesis
- The Parasite-Specific Trypanothione Metabolism of Trypanosoma and Leishmania
- Glutathione – Functions and Metabolism in the Malarial Parasite Plasmodium falciparum
- Oxidative Stress Caused by Inactivation of Glutathione Peroxidase and Adaptive Responses
- Versatility of Selenium Catalysis in PHGPx Unraveled by LC/ESI-MS/MS
- Modulation of the Chymotrypsin-Like Activity of the 20S Proteasome by Intracellular Redox Status: Effects of Glutathione Peroxidase-1 Overexpression and Antioxidant Drugs
- Microflora Trigger Colitis in Mice Deficient in Selenium-Dependent Glutathione Peroxidase and Induce Gpx2 Gene Expression
- Recruitment of the Interleukin-1 Receptor (IL-1RI)-Associated Kinase IRAK to the IL-1RI Is Redox Regulated
- Kinetics and Redox-Sensitive Oligomerisation Reveal Negative Subunit Cooperativity in Tryparedoxin Peroxidase of Trypanosoma brucei brucei
- Testis-Specific Expression of the Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx)
- Selective Recognition of Peptide Sequences by Glutathione Transferases: A Possible Mechanism for Modulation of Cellular Stress-Induced Signaling Pathways
- Biosynthesis of Trypanothione in Trypanosoma brucei brucei
- Transcriptional Regulation of Cytosol and Membrane Alanyl-Aminopeptidase in Human T Cell Subsets
- Regulation of Gene Transcription by a Constitutively Active Mutant of Activating Transcription Factor 2 (ATF2)
- Solvent Isotope Effect on the Reaction Catalysed by the Pyruvate Dehydrogenase Complex from Escherichia coli
- Selective Induction of Liver Parenchymal Cell Heme Oxygenase-1 in Selenium-Deficient Rats
