β2-Adrenergic Receptor Utilizes Distinct Interaction Interfaces to Selectively form Heterooligomers with a Subset of Bitter Taste Receptors.

ABSTRACT: G protein-coupled receptors (GPCRs) make up the largest receptor family in humans, which also constitute principal molecular targets for about 36% of approved drugs. Recent studies show that GPCRs can form heteromeric complexes with new molecular features. Little, however, is known about how human bitter taste receptors (T2Rs) form heteromeric receptors with other GPCRs. In this study, we combine biomolecular fluorescence complementation assays with methods for chemiluminescence imaging of cells, and find that β2-adrenergic receptor (β2AR) interacts with a subset of T2Rs, including T2R10, T2R14, T2R38, and T2R44, but selectively promotes cell membrane localization of only T2R14, T2R38, and T2R44. Furthermore, in silico modeling, coimmunoprecipitation, and immunofluorescence analysis indica

SUBMITTER: Peng YY 

PROVIDER: S-EPMC12329724 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature