Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6 (original) (raw)
- Letter
- Published: 23 November 2005
- Vanessa Redecke2,
- Blagoy Blagoev4,
- Irina Kratchmarova4,
- Li-Chung Hsu1,
- Gang G. Wang3,
- Mark P. Kamps3,
- Eyal Raz2,
- Hermann Wagner5,
- Georg Häcker5,
- Matthias Mann4 &
- …
- Michael Karin1
Nature volume 439, pages 204–207 (2006)Cite this article
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Abstract
Toll-like receptors (TLRs) are activated by pathogen-associated molecular patterns to induce innate immune responses and production of pro-inflammatory cytokines, interferons and anti-inflammatory cytokines1. TLRs activate downstream effectors through adaptors that contain Toll/interleukin-1 receptor (TIR) domains2, but the mechanisms accounting for diversification of TLR effector functions are unclear. To dissect biochemically TLR signalling, we established a system for isolating signalling complexes assembled by dimerized adaptors. Using MyD88 as a prototypical adaptor, we identified TNF receptor-associated factor 3 (TRAF3) as a new component of TIR signalling complexes that is recruited along with TRAF6. Using myeloid cells from TRAF3- and TRAF6-deficient mice, we show that TRAF3 is essential for the induction of type I interferons (IFN) and the anti-inflammatory cytokine interleukin-10 (IL-10), but is dispensable for expression of pro-inflammatory cytokines. In fact, TRAF3-deficient cells overproduce pro-inflammatory cytokines owing to defective IL-10 production. Despite their structural similarity, the functions of TRAF3 and TRAF6 are largely distinct. TRAF3 is also recruited to the adaptor TRIF (Toll/IL-1 receptor domain-containing adaptor-inducing IFN-β) and is required for marshalling the protein kinase TBK1 (also called NAK) into TIR signalling complexes, thereby explaining its unique role in activation of the IFN response.
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Acknowledgements
We thank J. Inoue for _Traf6_-deficient mice, M. Farrar for GyrB constructs, G. Oganesyan, S. K. Saha and G. Cheng for providing cells from TRAF3-deficient mice, T. Maniatis for anti-TBK1 antibodies and L. Pfeffer for L929 cells. H.H. and V.R. were supported by fellowships from the Deutsche Forschungsgemeinschaft (DFG). Work in the laboratories of M.P.K., E.R. and M.K. was supported by grants from the National Institutes of Health. M.K. is an American Cancer Society Research Professor.
Author information
Author notes
- Hans Häcker
Present address: Department of Infectious Diseases, St Jude Children's Research Hospital, 332 North Lauderdale Street, Memphis, Tennessee, 38105, USA
Authors and Affiliations
- Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, School of Medicine,
Hans Häcker, Li-Chung Hsu & Michael Karin - Department of Medicine,
Vanessa Redecke & Eyal Raz - Department of Pathology, University of California, 9500 Gilman Drive, California, 92093, San Diego, La Jolla, USA
Gang G. Wang & Mark P. Kamps - Center for Experimental BioInformatics (CEBI), Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230, Odense M, Denmark
Blagoy Blagoev, Irina Kratchmarova & Matthias Mann - Institute for Medical Microbiology, Immunology and Hygiene, Technische Universität München, Trogerstr. 9, D-81675, Munich, Germany
Hermann Wagner & Georg Häcker
Authors
- Hans Häcker
- Vanessa Redecke
- Blagoy Blagoev
- Irina Kratchmarova
- Li-Chung Hsu
- Gang G. Wang
- Mark P. Kamps
- Eyal Raz
- Hermann Wagner
- Georg Häcker
- Matthias Mann
- Michael Karin
Corresponding author
Correspondence toHans Häcker.
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Competing interests
Reprints and permissions information is available at npg.nature.com/reprintsandpermissions. The authors declare no competing financial interests.
Supplementary information
Supplementary Figure 1
Characterization of coumermycin-induced cell activation through the MyD88–GyrB- and TRAF6–GyrB fusion proteins. (PDF 559 kb)
Supplementary Figure 2
TRAF3 is recruited to TIR signalling complexes. (PDF 348 kb)
Supplementary Figure 3
Role of TRAF3 in TLR-induced signal transduction and gene regulation. (PDF 1212 kb)
Supplementary Figure 4
CpG-DNA-induced gene expression in wt and TRAF3-deficient BMDM. (PDF 12 kb)
Supplementary Figure 5
CpG-DNA- and LPS-induced gene regulation in wt and TRAF6-deficient BMDM and FLT3-ligand induced DCs. (PDF 10 kb)
Supplementary Figure 6
TRAF3-reconstitution of TRAF3-deficient HoxB8-immortalized myeloid progenitor cells rescues the CpG-DNA-induced IFN and IL-10 response. (PDF 156 kb)
Supplementary Figure Legends
Contains legends to accompany Supplementary Figures 1–6. (DOC 46 kb)
Supplementary Methods
Detailed description of the tandem affinity purification (TAP) technique used to purify MyD88-GyrB-TAP and description of the antibodies used in this work. (DOC 32 kb)
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Häcker, H., Redecke, V., Blagoev, B. et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6.Nature 439, 204–207 (2006). https://doi.org/10.1038/nature04369
- Received: 29 July 2005
- Accepted: 24 October 2005
- Published: 23 November 2005
- Issue date: 12 January 2006
- DOI: https://doi.org/10.1038/nature04369
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Editorial Summary
Viral response
The innate immune response, a vital defence against viral infections, is initiated when viral products induce type I interferon responses via the activation of Toll-like receptors and various cytoplasmic receptors. Two groups this week report on the properties of a molecule called TRAF3. Its function in immune cells was not previously known, but it is now shown to act as a convergence point for induction of the antiviral response by multiple viral recognition pathways.