Adenosine A2A receptors assemble into higher-order oligomers at the plasma membrane |
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| Authors: | Pierre-Alexandre Vidi Joseph MK Irudayaraj |
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| Institution: | a Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907-2051, United States
b Bindley Bioscience Center and Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, IN 47907-2051, United States |
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| 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)
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| 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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