Localization of the mouse 5-Hydroxytryptamine(1A) receptor in lipid Microdomains depends on its palmitoylation and is involved in receptor-mediated signaling

In the present study, we have used wild- type and palmitoylationdeficient mouse 5- hydroxytryptamine (1A) receptor ( 5- HT1A) receptors fused to the yellow fluorescent protein- and the cyan fluorescent protein ( CFP)- tagged alpha (i3) subunit of heterotrimeric G- protein to study spatiotemporal distribution of the 5- HT1Amediated signaling in living cells. We also addressed the question on the molecular mechanisms by which receptor palmitoylation may regulate communication between receptors and G i- proteins. Our data demonstrate that activation of the 5- HT1A receptor caused a partial release of G alpha(i) protein into the cytoplasm and that this translocation is accompanied by a significant increase of the intracellular Ca2+ concentration.