G Protein–Coupled Receptor Oligomerization

A direct and functional interaction between the trimeric G protein Go and Rab5 in G proteincoupled receptor signaling

G protein-coupled receptor oligomerization revisited: functional and pharmacological perspectives.

Most evidence indicates that, as for family C G protein-coupled receptors (GPCRs), family A GPCRs form homo- and heteromers. Homodimers seem to be a predominant species, with potential dynamic formation of higher-order oligomers, particularly tetramers. Although monomeric GPCRs can activate G proteins, the pentameric structure constituted by one GPCR homodimer and one heterotrimeric G protein m...

G-protein Coupled Receptor Dimerization

A growing body of evidence suggests that GPCRs exist and function as dimers or higher oligomers. The evidence for GPCR dimerization comes from biochemical, biophysical and functional studies. In addition, researchers have shown the occurrence of heterodimerization between different members of the GPCR family. Two receptors can interact with each other to make a dimer through their extracellular...

Activation of a G proteincoupled receptor by its endogenous ligand triggers the innate immune response of Caenorhabditis elegans

The innate defenses of the nematode Caenorhabditis elegans have diverged considerably from those of other animals. Perhaps most strikingly, C. elegans has lost the transcription factor NF-κB, key for defense in most animal species, and lacks functional orthologs of many known innate defense receptors1. On the other hand, core signaling pathways involved in innate immunity across a broad range o...

Muscarinic receptor oligomerization

G protein-coupled receptors (GPCRs) have been classically described as monomeric entities that function by binding in a 1:1 stoichiometric ratio to both ligand and downstream signalling proteins. However, in recent years, a growing number of studies has supported the hypothesis that these receptors can interact to form dimers and higher order oligomers although the molecular basis for these int...