Characterization of heteromeric complexes between chemokine (C-X-C motif) receptor 4 and α₁-adrenergic receptors utilizing intermolecular bioluminescence resonance energy transfer assays.

ABSTRACT: Recently, we reported that chemokine (C-X-C motif) receptor 4 (CXCR4) heteromerizes with α₁-adrenergic receptors (AR) on the cell surface of vascular smooth muscle cells, through which the receptors cross-talk. Direct biophysical evidence for CXCR4:α₁-AR heteromers, however, is lacking. Here we utilized bimolecular luminescence/fluorescence complementation (BiLC/BiFC) combined with intermolecular bioluminescence resonance energy transfer (BRET) assays in HEK293T cells to evaluate CXCR4:α_1a/b/d-AR heteromerization. Atypical chemokine receptor 3 (ACKR3) and metabotropic glutamate receptor 1 (mGlu₁R) were utilized as controls. BRET between CXCR4-RLuc (Renilla reniformis) and enhanced yellow fluorescent protein (EYFP)-tagged ACKR3 or α_1a/b/d

SUBMITTER: Gao X 

PROVIDER: S-EPMC7937191 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature