FEBS Letters
Volume 582, Issue 29 , Pages 3985-3990, 10 December 2008

Adenosine A2A receptors assemble into higher-order oligomers at the plasma membrane

Edited by Michael R. Bubb

  • Pierre-Alexandre Vidi

      Affiliations

    • Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907-2051, United States
    • ,
  • Jiji Chen

      Affiliations

    • Bindley Bioscience Center and Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, IN 47907-2051, United States
    • ,
  • Joseph M.K. Irudayaraj

      Affiliations

    • Bindley Bioscience Center and Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, IN 47907-2051, United States
    • ,
  • Val J. Watts

      Affiliations

    • Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907-2051, United States
    • Corresponding Author InformationCorresponding author. Fax: +1 765 494 1414.

Received 16 July 2008; received in revised form 10 September 2008; accepted 12 September 2008. published online 12 November 2008.

Abstract 

Oligomerization of G protein-coupled receptors (GPCRs) is known to play important roles in regulating receptor pharmacology and function. Whereas many bivalent GPCR interactions have been described, the stoichiometry and localization of GPCR oligomers are largely unknown. We have used bimolecular fluorescence complementation (BiFC) to study adenosine A2A receptor (A2AR) oligomerization. The data suggest specificity of the A2AR/A2AR interaction monitored by BiFC and proper sub-cellular localization of tagged receptors. Moreover, using a novel approach combining fluorescence resonance energy transfer and BiFC, we found that at least three A2A receptors assemble into higher-order oligomers at the plasma membrane in Cath.A differentiated neuronal cells.

Structured summary


MINT-6797156, MINT-6797142: A2AR (uniprotkb:P29274) physically interacts (MI:0218) with A2AR (uniprotkb:P29274) by bimolecular fluorescence complementation (MI:0809)

MINT-6797129: A2AR (uniprotkb:P29274) physically interacts (MI:0218) with A2AR (uniprotkb:P29274) by fluorescent resonance energy transfer (MI:0055)

Keywords: Bimolecular fluorescence complementation, Fluorescence (Forster) resonance energy transfer, Adenosine A2A receptor, G protein-coupled receptor, Higher-order oligomer, Neuronal cell

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PII: S0014-5793(08)00897-1

doi:10.1016/j.febslet.2008.09.062

FEBS Letters
Volume 582, Issue 29 , Pages 3985-3990, 10 December 2008

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