ArticleThe Journal of biological chemistry2012
Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 44 citations in OpenAlex.
- Pre-activation and gating pathway of AMPA receptors revealed by full and partial agonists.Nature structural & molecular biology · 2026Article
- Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor.Proteins · 2025Article
- Structural dynamics in α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor gating.Current opinion in structural biology · 2024Review
- Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Allosteric coupling of sub-millisecond clamshell motions in ionotropic glutamate receptor ligand-binding domains.Communications biology · 2021Article
- Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.Membranes · 2021Article
- Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain.Structure (London, England : 1993) · 2021Article
- Single molecule FRET methodology for investigating glutamate receptors.Methods in enzymology · 2021Article
- Structural Dynamics of Glutamate Signaling Systems by smFRET.Biophysical journal · 2020Review
- Mechanism of modulation of AMPA receptors by TARP-γ8.The Journal of general physiology · 2020Article
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Mechanistic Understanding of the Phosphorylation-Induced Conformational Rigidity at the AMPA Receptor C-terminal Domain.ACS omega · 2019Article
- The structural arrangement at intersubunit interfaces in homomeric kainate receptors.Scientific reports · 2019Article
- Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.Neuroscience letters · 2019Review
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.The journal of physical chemistry. B · 2019Article
- Single-Molecule FRET Methods to Study Glutamate Receptors.Methods in molecular biology (Clifton, N.J.) · 2019Article
- The structure-energy landscape of NMDA receptor gating.Nature chemical biology · 2017Article
- Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation.Cell reports · 2017Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
We have investigated the range of cleft closure conformational states that the agonist-binding domains of the α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors occupy when bound to a series of willardiine derivatives using single-molecule FRET. These studies show that the agonist-binding domain exhibits varying degrees of dynamics when bound to the different willardiines with differing efficacies. The chlorowillardiine- and nitrowillardiine-bound form of the agonist-binding domain probes a narrower range of cleft closure states relative to the iodowillardiine bound form of the protein, with the antagonist (αS)-α-amino-3-[(4-carboxyphenyl)methyl]-3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinepropanoic acid (UBP-282)-bound form exhibiting the widest range of cleft closure states. Additionally, the average cleft closure follows the order UBP-282 > iodowillardiine > chlorowillardiine > nitrowillardiine-bound forms of agonist-binding domain. These single-molecule FRET data, along with our previously reported data for the glutamate-bound forms of wild type and T686S mutant proteins, show that the mean currents under nondesensitizing conditions can be directly correlated to the fraction of the agonist-binding domains in the "closed" cleft conformation. These results indicate that channel opening in the AMPA receptors is controlled by both the ability of the agonist to induce cleft closure and the dynamics of the agonist-binding domain when bound to the agonist.
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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.