| First Author | Kramer JM | Year | 2006 |
| Journal | J Immunol | Volume | 176 |
| Issue | 2 | Pages | 711-5 |
| PubMed ID | 16393951 | Mgi Jnum | J:126608 |
| Mgi Id | MGI:3761739 | Doi | 10.4049/jimmunol.176.2.711 |
| Citation | Kramer JM, et al. (2006) Evidence for ligand-independent multimerization of the IL-17 receptor. J Immunol 176(2):711-5 |
| abstractText | 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. |
