Dimerization of G-protein-coupled receptors: roles in signal transduction.
Recently, many G-protein-coupled receptors (GPCRs) have been demonstrated to form constitutive dimers consisting of identical or distinct monomeric subunits. The discovery of GPCR dimerization has revealed a new level of molecular cross-talk between signalling molecules and may define a general mechanism that modulates the function of GPCRs under both physiological and pathological conditions. The heterodimerization between distinct GPCRs could be responsible for the generation of pharmacologically defined receptors for which no gene has been identified so far. Elucidating the role of dimerization in the activation processes of GPCRs will lead us to develop novel pharmaceutical agents that allosterically promote activation or inhibition of GPCR signalling.
Bai
Mei
M
Endocrine-Hypertension Division and Membrane Biology Program, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA. mbai@rics.bwh.harvard.edu
D000818:Animals; D019281:Dimerization; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D043562:Receptors, G-Protein-Coupled / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*
D043562:Receptors, G-Protein-Coupled; D019204:GTP-Binding Proteins