Medical Journals

Evidence for Ligand-independent Multimerization of the Il-17 Receptor.

Authors:
  • Kramer Jill M
  • Yi Ling
  • Shen Fang
  • Maitra Amarnath
  • Jiao Xuanmao
  • Jin Tian
  • Gaffen Sarah L

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


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.

The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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