Evidence for Ligand-independent Multimerization of the Il-17 Receptor.
From: Department of Oral Biology, School of Dental Medicine, University at Buffalo, State University of New York, Buffalo, NY 14214, USA.
Journal of immunology (Baltimore, Md. : 1950)
- Publish Date: Jan 2006
- ISSN: 0022-1767
- Volume: 176
- Issue: 2
- Pages: 711-5
- Medium: Print
- Language: English
- Citation (JAMA): Kramer Jill M, Yi Ling, Shen Fang, et al. Evidence for Ligand-independent Multimerization of the Il-17 Receptor.. J. Immunol. Jan 2006;176:711-5
Abstract
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.
Mesh Headings (Keywords): Animals, Bacterial Proteins, Cell Line, Fluorescence Resonance Energy Transfer, Green Fluorescent Proteins, Humans, Interleukin-17, Ligands, Luminescent Proteins, Mice, Models, Molecular, Multiprotein Complexes, Protein Structure, Quaternary, Protein Subunits, Receptors, Interleukin, Recombinant Fusion Proteins, Transfection
Check for Full Text / PubMed Unique Identifier (PMID): 16393951
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