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.

Apoptotic cells release molecules to recruit macrophages, but do not cause inflammation because they also secrete AMP that functions as a ‘calm down’ signal.

Cholesterol exhibits transient interaction with A2AR and regulates receptor conformational equilibria through indirect membrane effects.

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.

Targeting CD73 not only enhances anti-tumor immunity but also disrupts tumor cell metabolism and hinders poly ADP ribose polymerase (PARP) activity, thus unveiling novel opportunities for combination cancer treatments.

Circulating human primed innate lymphoid cell precursors have the potential to functionally induce adhesion molecules' expression in endothelial cells and possibly support the immune cells' infiltration into the tumor site.

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 C-terminus of A_2A receptor drives oligomer formation via an intricate network of disulfide bonds, hydrogen bonds, electrostatic interactions, and hydrophobic interactions, all of which are enhanced by depletion interactions.

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.