Evidence for ligand-independent multimerization of the IL-17 receptor.


IL-17 and its receptor are founding members of a novel inflammatory cytokine family. To date, only one IL-17 receptor subunit has been identified, termed IL-17RA. All known cytokine receptors consist of a complex of multiple subunits. Although IL-17-family cytokines exist as homodimers, the configuration and stoichiometry of the IL-17R complex remain unknown. We used fluorescence resonance energy transfer (FRET) to determine whether IL-17RA subunits multimerize, and, if so, whether they are preassembled in the plasma membrane. HEK293 cells coexpressing IL-17RA fused to cyan or yellow fluorescent proteins (CFP or YFP) were used to evaluate FRET before and after IL-17A or IL-17F treatment. In the absence of ligand, IL-17RA molecules exhibited significant specific FRET efficiency, demonstrating that they exist in a multimeric, preformed receptor complex. Strikingly, treatment with IL-17A or IL-17F markedly reduced FRET efficiency, suggesting that IL-17RA subunits within the IL-17R complex undergo a conformational change upon ligand binding.


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@article{Kramer2006EvidenceFL, title={Evidence for ligand-independent multimerization of the IL-17 receptor.}, author={Jill M. Kramer and Ling Ka Yi and Fang Shen and Amarnath Maitra and Xuanmao Jiao and Tian Jin and Sarah L. Gaffen}, journal={Journal of immunology}, year={2006}, volume={176 2}, pages={711-5} }