Organization of higher-order oligomers of the serotonin1A receptor explored utilizing homo-FRET in live cells, Biophys

ABSTRACT The serotonin1A receptor is a representative memb target. The possible role of GPCR oligomerization in receptor func ization state of serotonin1A receptors using homo-FRET and fluor a reduction in fluorescence anisotropy and provides a superior ap offers the possibility of detecting higher-order oligomers. On the b ee e o gom ula d c pto CR (2). The serotonin1A (5-HT1A) receptor is an important complications arising from the use of receptors conjugated between like fluorophores and therefore requires only the nanometer scale and thus is sensitive to protein oligo-merization. The excitation and emission spectra of fluoro-FRET, fluorescence resonance energy transfer; GPCR, G-protein coupled receptor; MbCD, methyl-b-cyclodextrin; p-MPPI, 4-(20-methoxy)-phenyl-Biophysical Journal Volume 100 January 2011 361–368 361 2011 by the Biophysical Societyphores exhibiting homo-FRET should have considerable1-[