Combining powerful simulation methods uncovers the structural and dynamical changes driving G protein activation in atomic detail, revealing the allosteric network that triggers GDP release and reconciling diverse experimental data.

The adenosine A2a receptor couples to the heterotrimeric G protein Gs using both conserved contacts seen in other complexes and, in addition, novel contacts to the beta subunit of the G protein.

Sensory hair cells in the inner ear use inhibitory G proteins with different regulators at different stages of development to break symmetry, adopt a proper orientation, and grow stereocilia.

Heterotrimeric G proteins are coupled to and regulate plant receptor signaling, which allows optimum immune activation and enhances the production of reactive oxygen species.

The ciliary G-protein Arl13B – which is often mutated in Joubert syndrome – is the Guanine nucleotide exchange factor for the G-protein Arl3 and exclusively localizes to cilia.

A G protein in striatal neurons forms preassembled complexes with its downstream enzyme, adenylyl cyclase, which has implications for the pathophysiology of movement disorders.

Linking deep mutational scanning with engineered transcriptional reporters in human cell lines establishes a generalizable method for exploring pharmacogenomics, structure, and function across broad classes of drug receptors.

The GPCR-G protein coupling map and selectivity insights will catalyze advances in receptor research, cellular signaling, and drug discovery exploiting G protein signaling bias to design safer drugs.

Latrophilin-2 G protein coupling is required in axons but not target neurons for neural circuit assembly in the mouse hippocampus.

Heterotrimeric G-proteins can be switched on not only by G-protein-coupled receptors but also by cytoplasmic proteins, resulting in different signaling mechanisms in cells depending on the specific type of activator.