Heterodimerization of G-protein-coupled receptors: pharmacology, signalingand trafficking

Although classical models predict that G-protein-coupled receptors (GPCRs) function as monomers, several recent studies acknowledge that GPCRs exist a s dimeric or oligomeric complexes. In addition to homodimers, heterodimers between members of the GPCR family (both closely and distantly related) hav e been reported. In some cases heterodimerization is required for efficient agonist binding and signaling, and in others heterodimerization appears to lead to the generation of novel binding sites. In this article, the techni ques used to study GPCR heterodimers, and the,novel pharmacology' and funct ional implications resulting from heterodimerization will be discussed.