ArticleProceedings of the National Academy of Sciences of the United States of America2021
High-mass MALDI-MS unravels ligand-mediated G protein-coupling selectivity to GPCRs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Artificial intelligence-driven integration of multi-biofluid omics and clinical phenotype enables stratification of endometrial cancer.Cell reports. Medicine · 2026Article
- Integrating Functional Response and Target Binding for Mechanism-Centered Drug Screening by High-Mass MALDI-MS.ACS central science · 2026Article
- Conformational Heterogeneity Underlying Divergent Signaling in Class A G Protein-Coupled Receptors.ACS pharmacology & translational science · 2025Review
- Unique Role of Intracellular Perinuclear βCirculation · 2025Article
- Deciphering molecular determinants of GPBAR1-Gs protein interactions by HDX-MS and cryo-EM.Scientific reports · 2025Article
- Evaluation of Drug Responses to Human βACS omega · 2023Article
- Finding the Perfect Fit: Conformational Biosensors to Determine the Efficacy of GPCR Ligands.ACS pharmacology & translational science · 2022Review
- ATRAP, a receptor-interacting modulator of kidney physiology, as a novel player in blood pressure and beyond.Hypertension research : official journal of the Japanese Society of Hypertension · 2022Review
- High-mass MALDI-MS unravels ligand-mediated G protein-coupling selectivity to GPCRs.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
G protein-coupled receptors (GPCRs) are important pharmaceutical targets for the treatment of a broad spectrum of diseases. Although there are structures of GPCRs in their active conformation with bound ligands and G proteins, the detailed molecular interplay between the receptors and their signaling partners remains challenging to decipher. To address this, we developed a high-sensitivity, high-throughput matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) method to interrogate the first stage of signal transduction. GPCR-G protein complex formation is detected as a proxy for the effect of ligands on GPCR conformation and on coupling selectivity. Over 70 ligand-GPCR-partner protein combinations were studied using as little as 1.25 pmol protein per sample. We determined the selectivity profile and binding affinities of three GPCRs (rhodopsin, beta-1 adrenergic receptor [β1AR], and angiotensin II type 1 receptor) to engineered Gα-proteins (mGs, mGo, mGi, and mGq) and nanobody 80 (Nb80). We found that GPCRs in the absence of ligand can bind mGo, and that the role of the G protein C terminus in GPCR recognition is receptor-specific. We exemplified our quantification method using β1AR and demonstrated the allosteric effect of Nb80 binding in assisting displacement of nadolol to isoprenaline. We also quantified complex formation with wild-type heterotrimeric Gα
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