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Updated: Jul 1, 2025
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
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ADGRG1, an adhesion G protein-coupled receptor, forms oligomers.
Orkun Cevheroğlu1, Berkay Demirbaş2, Dilara Öğütcü2
1Stem Cell Institute, Ankara University, Çankaya, Turkey.
The FEBS Journal
|March 12, 2024
Summary
Adhesion G protein-coupled receptor G1 (ADGRG1) forms homo-oligomers on the cell surface. Interactions involving the N-terminal fragment, specifically the Stachel motif, influence these G protein-coupled receptor complexes.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- G protein-coupled receptors (GPCRs) are increasingly recognized to function as oligomers, not monomers.
- Adhesion GPCRs (aGPCRs) are a unique class with complex N-terminal fragments (NTFs) and activation mechanisms.
- The functional significance of GPCR oligomerization, especially within aGPCRs, remains largely unexplored.
Purpose of the Study:
- To investigate the homo-oligomerization of adhesion G protein-coupled receptor G1 (ADGRG1).
- To determine the role of ADGRG1's N-terminal fragments (NTFs) in forming these receptor complexes.
- To explore how specific motifs within the NTF influence receptor complex conformation.
Main Methods:
- Utilized bioluminescence energy transfer (BRET) to detect receptor proximity.
- Employed Förster resonance energy transfer (FRET) to study homo-oligomerization.
- Analyzed the involvement of the N-terminal fragment (NTF) and Stachel motif in ADGRG1 complex formation.
Main Results:
- Demonstrated that ADGRG1 forms homo-oligomers on the plasma membrane.
- Provided evidence for 7-transmembrane domain-driven oligomerization.
- Indicated that Stachel motif interactions modulate the conformation of ADGRG1 homo-oligomers.
Conclusions:
- ADGRG1 functions as a homo-oligomer, driven by its transmembrane domains.
- The N-terminal fragment, particularly the Stachel motif, plays a crucial role in regulating ADGRG1 complex structure and potentially function.
- These findings contribute to understanding the structural basis of adhesion GPCR signaling and oligomerization.
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