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An adenylyl cyclase isoform is shown to dynamically traffic to endosomes after activation by G protein in mammalian cells, contributing to cellular cAMP signaling by internalized GPCRs.

Daple is a guanine nucleotide-exchange factor (GEF) for trimeric G proteins that enables Wnt/Frizzled receptors to transactivate G proteins during non-canonical Wnt signaling.

Development, validation, and use of an effector membrane translocation biosensor platform reveals G protein coupling selectivity signatures for 100 GPCRs that range from remarkable selectivity to full promiscuity toward the different G protein subtypes.

The G protein subunits Gβγ and the signaling lipid PIP2 are simultaneously needed to activate the potassium ion channel GIRK2 to control the voltage across a lipid bilayer, while sodium ions modulate these molecules' effects.

Serine and threonine phosphorylation sites work in concert to provide rapid and reproducible desensitization of the G-protein coupled receptor rhodopsin.

Heterotrimeric G proteins are less abundant on endosomes and organelles than on the plasma membrane.

Hydrogen-Deuterium exchange experiments show that Ric-8A induces similar dynamic changes in the structure of Gα as G protein-coupled receptors, yet protects a larger surface of the nucleotide-binding Ras domain.

The structural role of PIP2 in opening the G-protein-gated K⁺ channel is revealed.

Determining how GIRK2 activity depends on the concentration of Gβγ subunits in lipid membranes at different Na⁺ concentrations has allowed the Gβγ concentration generated during GABA_B activation in neurons to be estimated.

The vasopressin type 2 receptor promotes dual Gα_s and Gα_q/11 signaling at early endosomes in β-arrestin-dependent and -independent manners.