ArticleeLife2019
Conformational dynamics between transmembrane domains and allosteric modulation of a metabotropic glutamate receptor.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 46 citations in OpenAlex.
- Structural basis of active state coupling of metabotropic glutamate receptor 8 to beta-arrestins.Nature communications · 2026Article
- Configurational diversity of metabotropic glutamate receptor complexes with beta-arrestins.Nature communications · 2026Article
- Structural basis of positive allosteric modulation of metabotropic glutamate receptor activation and internalization.Nature communications · 2024Article
- G protein-coupled receptors (GPCRs): advances in structures, mechanisms, and drug discovery.Signal transduction and targeted therapy · 2024Review
- Synaptic plasticity via receptor tyrosine kinase/G-protein-coupled receptor crosstalk.Cell reports · 2024Article
- Structural insights into dimerization and activation of the mGlu2-mGlu3 and mGlu2-mGlu4 heterodimers.Cell research · 2023Article
- Concerted conformational changes control metabotropic glutamate receptor activity.Science advances · 2023Article
- Kinetic fingerprinting of metabotropic glutamate receptors.Communications biology · 2023Article
- Detecting and measuring of GPCR signaling - comparison of human induced pluripotent stem cells and immortal cell lines.Frontiers in endocrinology · 2023Review
- Leveraging Baird aromaticity for advancement of bioimaging applications.Journal of physical organic chemistry · 2023Article
- Membrane-mediated protein interactions drive membrane protein organization.Nature communications · 2022Article
- Control of GαScience advances · 2022Article
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- Sulfonated red and far-red rhodamines to visualize SNAP- and Halo-tagged cell surface proteins.Organic & biomolecular chemistry · 2022Article
- Conformational fingerprinting of allosteric modulators in metabotropic glutamate receptor 2.eLife · 2022Article
- Subsynaptic mobility of presynaptic mGluR types is differentially regulated by intra- and extracellular interactions.Molecular biology of the cell · 2022Article
- Article
- Structural and compositional diversity in the kainate receptor family.Cell reports · 2021Article
- Asymmetry is central to excitatory glutamate receptor activation.Nature structural & molecular biology · 2021Article
- Selective Photoswitchable Allosteric Agonist of a G Protein-Coupled Receptor.Journal of the American Chemical Society · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Metabotropic glutamate receptors (mGluRs) are class C, synaptic G-protein-coupled receptors (GPCRs) that contain large extracellular ligand binding domains (LBDs) and form constitutive dimers. Despite the existence of a detailed picture of inter-LBD conformational dynamics and structural snapshots of both isolated domains and full-length receptors, it remains unclear how mGluR activation proceeds at the level of the transmembrane domains (TMDs) and how TMD-targeting allosteric drugs exert their effects. Here, we use time-resolved functional and conformational assays to dissect the mechanisms by which allosteric drugs activate and modulate mGluR2. Single-molecule subunit counting and inter-TMD fluorescence resonance energy transfer measurements in living cells reveal LBD-independent conformational rearrangements between TMD dimers during receptor modulation. Using these assays along with functional readouts, we uncover heterogeneity in the magnitude, direction, and the timing of the action of both positive and negative allosteric drugs. Together our experiments lead to a three-state model of TMD activation, which provides a framework for understanding how inter-subunit rearrangements drive class C GPCR activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.