Metabotropic glutamate receptor homo- and heterodimers exhibit distinct responses to orthosteric and allosteric ligands.

ABSTRACT: Metabotropic glutamate receptors (mGlus) are obligate dimer G protein-coupled receptors that can all homodimerize and heterodimerize in select combinations. Responses of mGlu heterodimers to selective ligands, including orthosteric agonists and allosteric modulators, are largely unknown. The pharmacological properties of each group II and III mGlu homodimer (except the exclusively retinally expressed mGlu6) and several heterodimers were examined when stochastically assembled in HEK293T cells, or specifically measured using an improved G protein-mediated bioluminescence resonance energy transfer assay employing complemented fragments of Nanoluciferase. Stochastically assembled receptors adopted unique signaling characteristics. Some favored the potency, efficacy, or signaling kinetics of a

SUBMITTER: McCullock TW 

PROVIDER: S-EPMC12597640 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature