Class A G protein‐coupled receptors assemble into functional higher‐order hetero‐oligomers
| Autor: | Garrett Enten, Anthony J. DeSantis, Matthias Majetschak, Xianlong Gao |
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| Rok vydání: | 2021 |
| Předmět: |
Receptors
CXCR4 Receptors Vasopressin Chemokine Adrenergic receptor Protein Conformation Recombinant Fusion Proteins Biophysics Gene Expression macromolecular substances environment and public health Biochemistry Article 03 medical and health sciences Bimolecular fluorescence complementation Chemokine receptor Bacterial Proteins Genes Reporter Structural Biology Receptors Adrenergic alpha-1 Fluorescence Resonance Energy Transfer Genetics Humans Protein Interaction Domains and Motifs Luciferases Receptor Molecular Biology 030304 developmental biology G protein-coupled receptor Receptors CXCR 0303 health sciences Arginine vasopressin receptor 1A biology Chemistry 030302 biochemistry & molecular biology HEK 293 cells Cell Biology Chemokine CXCL12 Kinetics Luminescent Proteins HEK293 Cells biology.protein Protein Multimerization Plasmids Protein Binding |
| Zdroj: | FEBS Lett |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.14135 |
| Popis: | Although class A seven-transmembrane-helix (7TM) receptor hetero-oligomers have been proposed, information on the assembly and function of such higher-order hetero-oligomers is not available. Utilizing bioluminescence resonance energy transfer (BRET), bimolecular luminescence/fluorescence complementation (BiLC/BiFC) and BiLC/BiFC BRET in HEK293T cells, we provide evidence that chemokine (C-X-C motif) receptor 4 (CXCR4), atypical chemokine receptor 3 (ACKR3), α(1a)-adrenoceptor (α(1a)-AR), and arginine vasopressin receptor 1A (AVPR1A) form hetero-oligomers composed of 2-4 different protomers. We show that hetero-oligomerization per se and ligand binding to individual protomers regulate agonist-induced coupling to the signaling transducers of interacting receptor partners. Our findings support the concept that receptor hetero-oligomers form supramolecular machineries with molecular signaling properties distinct from the individual protomers. These findings provide a mechanism for the phenomenon of context-dependent receptor function. |
| Databáze: | OpenAIRE |
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