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

LOV2GIVe allows to activate Gi proteins non-invasively with innocuous blue light based on a design principle unrelated to light-activated GPCRs (metazoan opsins), thereby expanding the range of potential experimental applications.

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.

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.

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.

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.

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.

Molecular genetics identifies a novel microglial pathway essential for mouse brain development and a previously unknown anti-inflammatory activity of monomeric amyloid β that activates this pathway.

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.