DETECTION OF THE HOMO-OLIGOMERIZATION OF ADGRE2/EMR2 USING BRET AND FRET.

Date

2023-6-12

Author

Öğütcü, Dilara

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G protein-coupled receptors (GPCRs) mediate a large variety of cellular responses and are the largest family of membrane-bound receptors. GPCRs are known to form homo- and/or hetero- oligomeric complexes in live cells. These complexes affect receptor maturation, trafficking, and signaling. Adhesion G protein-coupled receptors (aGPCRs), is the second largest sub-family of GPCRs in mammals. It is known that they interact with extracellular matrix proteins and ligands on the cell surface that plays a role in tissue and organ development. Nevertheless, it is not fully understood whether aGPCRs form oligomeric structures. In the current study, a member of the aGPCRs, ADGRE2 / EMR2, and one of its isoforms ADGRE2(125) / EMR2(125) were tagged with fluorescent or bioluminescent proteins to study homo-oligomerization using BRET and FRET. ADGRE2 is mostly expressed in the immune cells, and its expression is highly controlled during monocyte/macrophage differentiation. Moreover, ADGRE2 is related to an autosomal dominant disease called vibratory urticaria. Patients suffer from erythema and edema on their skin because of mechanical stimuli. However, the function of this receptor is not well-understood. Since dimerization and oligomerization can be important in the trafficking of many GPCRs, understanding if these GPCRs oligomerize could help us study their unknown functions with ease. This study indicates that ADGRE2 and ADGRE2(125) isoforms tend to be found in different oligomeric states in the plasma membrane. Therefore, our findings are indications of the role of extracellular domains on ADGRE2/EMR2 homo-oligomerization. The results of this study will help us to investigate further the effect of receptor oligomerization on physiology.

Subject Keywords

Adhesion GPCR, ADGRE2, EMR2, BRET, FRET, Adezyon GPKR, ADGRE2, EMR2, BRET, FRET

URI

https://hdl.handle.net/11511/104420

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Graduate School of Natural and Applied Sciences, Thesis