期刊
JOURNAL OF IMMUNOLOGY
卷 176, 期 2, 页码 711-715出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.176.2.711
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- Intramural NIH HHS Funding Source: Medline
- NIAMS NIH HHS [R21 AR050458, AR050458] Funding Source: Medline
- NIDCR NIH HHS [F30 DE014831, F30 DE014831-04, DE014831] Funding Source: Medline
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-17P 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-IM subunits within the IL-17R complex undergo a conformational change upon ligand binding.
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