Organization of higher-order oligomers of the serotonin₁(A) receptor explored utilizing homo-FRET in live cells.

ABSTRACT: The serotonin₁(A) receptor is a representative member of the GPCR superfamily and serves as an important drug target. The possible role of GPCR oligomerization in receptor function is an active area of research. We monitored the oligomerization state of serotonin₁(A) receptors using homo-FRET and fluorescence lifetime measurements. Homo-FRET is estimated by a reduction in fluorescence anisotropy and provides a superior approach for exploring oligomerization. In addition, homo-FRET offers the possibility of detecting higher-order oligomers. On the basis of an observed increase in fluorescence anisotropy upon progressive photobleaching and analysis of the difference between the extrapolated anisotropy and the predicted anisotropy of an immobile monomer, we propose the presence of constitutiv

SUBMITTER: Ganguly S 

PROVIDER: S-EPMC3021661 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature