Oligomerization of opioid receptors with beta 2-adrenergic receptors: A role in trafficking and mitogen-activated protein kinase activation

摘要: G-protein-coupled receptors (GPCRs) have recently joined the list of cell surface that dimerize. Dimerization has been shown to alter ligand-binding, signaling, and trafficking properties these receptors. Recent studies GPCRs heterodimerize with closely related members, resulting in modulation their function. In this study, we attempted determine whether members GPCR superfamilies couple different families G-proteins can associate form oligomers. We chose β2 adrenergic receptor couples stimulatory δ & κ opioid inhibitory G-proteins. undergo robust agonist-mediated endocytosis, whereas do not. find when coexpressed, heteromeric complexes both This heterooligomerization does not significantly ligand binding or coupling However, it affects For example, receptors, coexpressed isoproterenol-mediated endocytosis. Conversely, cells etorphine-mediated neither opioid- nor Moreover, exhibit a substantial decrease isoproterenol-induced phosphorylation mitogen-activated protein kinases. Taken together, results provide direct evidence heteromerization types G-proteins, which signal transduction.