The structure of a light-sensitive G protein-coupled receptor in complex with a Gi-protein heterotrimer provides a structural foundation for the role of the receptor C-terminal tail in scaffolding and signaling.

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

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.

A single kinetic step in the G protein activation cycle determines whether a G protein-coupled receptor activates G protein-gated K⁺ channels or not.

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

Single molecule reconstitution of PI3Kβ synergistic activation reveals mechanism for rapid PI(3,4,5)P₃ production during immune cell signaling.

Pro-nociceptive and pro-inflammatory TRPM3 (transient receptor potential melastatin 3) channels, expressed in somatosensory neurons, are inhibited by activation of Gαi-coupled receptors, such as µ-opioid receptors, in vitro and in vivo.

Electrophysiological experiments, Ca²⁺ imaging, and behavioral studies in mice identify the TRPM3 ion channel as a novel target of G-protein βγ subunits.

Atomic details on structural organization and conformational dynamics of the key regulator of neuronal signaling shed light on its allosteric regulation and role in regulating cellular pathways.

The cryo-EM structure of ET_B-G_i complex, obtained using the Fusion-G system, provides insights into the distinct activation mechanism and G-protein promiscuity of ET_B, aiding in the design of ET_B agonists for therapeutic applications.