Vidi Pierre-Alexandre, Chen Jiji, Irudayaraj Joseph M K, Watts Val J
Department of Medicinal Chemistry, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907-2051, United States.
FEBS Lett. 2008 Dec 10;582(29):3985-90. doi: 10.1016/j.febslet.2008.09.062. Epub 2008 Nov 12.
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.
已知G蛋白偶联受体（GPCRs）的寡聚化在调节受体药理学和功能方面发挥重要作用。尽管已经描述了许多二价GPCR相互作用，但GPCR寡聚体的化学计量和定位在很大程度上尚不清楚。我们使用双分子荧光互补（BiFC）来研究腺苷A(2A)受体（A(2A)R）的寡聚化。数据表明通过BiFC监测的A(2A)R/A(2A)R相互作用具有特异性，并且标记受体具有适当的亚细胞定位。此外，使用一种结合荧光共振能量转移和BiFC的新方法，我们发现在Cath.A分化的神经元细胞中，至少三个A(2A)受体在质膜上组装成高阶寡聚体。
