Adenosine A(2A) receptors assemble into higher-order oligomers at the plasma membrane.
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 A(2A) receptor (A(2A)R) oligomerization. The data suggest specificity of the A(2A)R/A(2A)R 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 A(2A) receptors assemble into higher-order oligomers at the plasma membrane in Cath.A differentiated neuronal cells.
Vidi
Pierre-Alexandre
PA
Department of Medicinal Chemistry, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907-2051, United States.
Chen
Jiji
J
Irudayaraj
Joseph M K
JM
Watts
Val J
VJ
D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D009474:Neurons / Q000378:metabolism* / Q000648:ultrastructure; D043705:Receptor, Adenosine A2A / Q000235:genetics / Q000378:metabolism*
D043705:Receptor, Adenosine A2A