Interactions among the components of the interleukin-10 receptor complex

• Published in: Biochemical and biophysical research communications 2006-02, Vol.340 (2), p.377-385
• Main Authors: Krause, Christopher D., Mei, Erwen, Mirochnitchenko, Olga, Lavnikova, Natasha, Xie, Junxia, Jia, Yiwei, Hochstrasser, Robin M., Pestka, Sidney
• Format: Article
• Language: English
• Subjects: Animals; Cell Membrane - metabolism; Chlorocebus aethiops; COS Cells; Cytokines; Fluorescence Resonance Energy Transfer; Interactions; Interferon gamma Receptor; Interleukin-10; Interleukin-10 - metabolism; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Protein Subunits - metabolism; Receptors; Receptors, Interferon - chemistry; Receptors, Interferon - metabolism; Receptors, Interleukin - chemistry; Receptors, Interleukin - metabolism; Receptors, Interleukin-10; Signal transduction
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2005.11.182

We used fluorescence resonance energy transfer previously to show that the interferon-γ (IFN-γ) receptor complex is a preformed entity mediated by constitutive interactions between the IFN-γR2 and IFN-γR1 chains, and that this preassembled entity changes its structure after the treatment of cells with IFN-γ. We applied this technique to determine the structure of the interleukin-10 (IL-10) receptor complex and whether it undergoes a similar conformational change after treatment of cells with IL-10. We report that, like the IFN-γ receptor complex, the IL-10 receptor complex is preassembled: constitutive but weaker interactions occur between the IL-10R1 and IL-10R2 chains, and between two IL-10R2 chains. The IL-10 receptor complex undergoes no major conformational changes when cells are treated with cellular or Epstein–Barr viral IL-10. Receptor complex preassembly may be an inherent feature of Class 2 cytokine receptor complexes.