Despite recent advances in determining the structure of G protein-coupled receptors (GPCRs), many mechanistic details of receptor signaling remain elusive, e.g. interactions with other proteins, lipids and membrane components. The canonical signaling model posits a single receptor to ligand in signaling. This model has been tested using both in vitro and in vivo systems, but cannot account fully for all observed signaling behavior. Recently, the molecular mechanism and downstream effects of cross-talk between receptor molecules has become an active area of study, using computational, in vitro and in vivo models.Here, we present in vivo downstream signaling data for dimerized pairs of human GPCRs, recorded with FRET-based receptor proximity assays via an engineered strain of yeast. The effects of GPCR interaction are further isolated and characterized in liposomes in vitro. Together, the data from these studies should lead to novel means of targeting GPCRs to more precisely control cell signaling responses.

Recombinant GPCR oligomerization effects on downstream signaling in yeast

245th National Meeting (2013)

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