Journal
FEBS LETTERS
Volume 582, Issue 29, Pages 3985-3990Publisher
WILEY
DOI: 10.1016/j.febslet.2008.09.062
Keywords
Bimolecular fluorescence complementation; Fluorescence (Forster) resonance energy transfer; Adenosine A(2A) receptor; G protein-coupled receptor; Higher-order oligomer; Neuronal cell
Funding
- Purdue University
- NIMH [MH060397]
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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.
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