The gβγ Dimer as a Novel Source of Selectivity in G-Protein Signaling: GGL-ing AT CONVENTION

A model depicting a possible Gα–GDP–Gβ₅–R7 heterotrimer coupled to a GPCR. GDP-bound Gα would undergo ligand-induced nucleotide exchange when coupled with a Gβ₅–R7 dimer. The Gβ₅–R7 complex would be tethered to the membrane via binding of R9AP (or an R9AP-like molecule) to the DEP domain of the RGS protein. Upon activation, the RGS domain of the Gβ₅–R7 complex would be conveniently localized to accelerate the hydrolysis of GTP to GDP.