Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that  receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the formations of various aggregated receptor states. Our results from model simulations imply that the receptor aggregation processes can govern the signaling activity in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus . More broadly, our work provides concrete modeling principles to explore general relations between receptor aggregation and various signaling properties .
Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observable states of receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the vector representation of various unobserved aggregated receptor states. Our results from model simulations imply that receptor aggregation processes can govern cooperative effects in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus .
A
observable states of
R
formations of various
vector representation of various unobserved
D
the
R
the signaling activity
cooperative effects
D
. More broadly, our work provides concrete modeling principles to explore general relations between receptor aggregation and various signaling properties