TY - JOUR
T1 - Adenosine A2A receptors assemble into higher-order oligomers at the plasma membrane
AU - Vidi, Pierre Alexandre
AU - Chen, Jiji
AU - Irudayaraj, Joseph M.K.
AU - Watts, Val J.
N1 - Funding Information:
This project was funded by Purdue University and NIMH grant award MH060397 to V.J.W. The pBiFC vectors were kindly provided by Dr. C.-D. Hu (Purdue University). The mCherry-Mem, YFP-Endo, YFP-ER, and YFP-golgi constructs were gifts from Dr. C. Berlot (Weis Center for Research). The C5V and CTV constructs were kindly provided by Dr. S. Vogel (NIH).
PY - 2008/12/10
Y1 - 2008/12/10
N2 - 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).
AB - 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).
KW - Adenosine A receptor
KW - Bimolecular fluorescence complementation
KW - Fluorescence (Forster) resonance energy transfer
KW - G protein-coupled receptor
KW - Higher-order oligomer
KW - Neuronal cell
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U2 - 10.1016/j.febslet.2008.09.062
DO - 10.1016/j.febslet.2008.09.062
M3 - Article
C2 - 19013155
AN - SCOPUS:56649106450
SN - 0014-5793
VL - 582
SP - 3985
EP - 3990
JO - FEBS Letters
JF - FEBS Letters
IS - 29
ER -