ArticleThe Journal of biological chemistry2010
On the mechanisms of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor binding to glutamate and kainate.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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
22 citing papers in PubMed, 26 citations in OpenAlex.
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- The structural arrangement at intersubunit interfaces in homomeric kainate receptors.Scientific reports · 2019Article
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- Population Shift Mechanism for Partial Agonism of AMPA Receptor.Biophysical journal · 2019Article
- Role of the Ion Channel Extracellular Collar in AMPA Receptor Gating.Scientific reports · 2017Article
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
- Structure of an agonist-bound ionotropic glutamate receptor.Science (New York, N.Y.) · 2014Article
- Thermodynamics and mechanism of the interaction of willardiine partial agonists with a glutamate receptor: implications for drug development.Biochemistry · 2014Article
- Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.The Journal of biological chemistry · 2013Article
- Functional insights from glutamate receptor ion channel structures.Annual review of physiology · 2013Review
- An integrated catch-and-hold mechanism activates nicotinic acetylcholine receptors.The Journal of general physiology · 2012Article
- The loss of an electrostatic contact unique to AMPA receptor ligand binding domain 2 slows channel activation.Biochemistry · 2012Article
- GluN1-specific redox effects on the kinetic mechanism of NMDA receptor activation.Biophysical journal · 2011Article
- Mechanisms of modal activation of GluA3 receptors.Molecular pharmacology · 2011Article
- Not all desensitizations are created equal: physiological evidence that AMPA receptor desensitization differs for kainate and glutamate.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Glutamate pharmacology and metabolism in peripheral primary afferents: physiological and pathophysiological mechanisms.Pharmacology & therapeutics · 2011Review
- Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.Current opinion in neurobiology · 2011Review
- Structural biology: One domain, multiple conformations.Nature chemical biology · 2011Article
- The hidden energetics of ligand binding and activation in a glutamate receptor.Nature structural & molecular biology · 2011Article
- Structural landscape of isolated agonist-binding domains from single AMPA receptors.Nature chemical biology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) subtype of ionotropic glutamate receptors mediates much of the fast excitatory neurotransmission in the central nervous system. The ability of these receptors to shape such responses appears to be due in part to dynamic processes induced by agonists in the ligand-binding domain. Previous studies employing fluorescence spectroscopy and whole cell recording suggest that agonist binding is followed by sequential transitions to one or more distinct conformational states. Here, we used hydrogen-deuterium exchange to determine the mechanisms of binding of glutamate and kainate (full and partial agonists, respectively) to a soluble ligand-binding domain of GluR2. Our results provide a structural basis for sequential state models of agonist binding and the free energy changes of the associated state-to-state transitions. For glutamate, a multi-equilibrium binding reaction was discerned involving distinct ligand docking, domain isomerization, and lobe-locking steps. In contrast, kainate binding involves a simpler dock-isomerization process in which the isomerization equilibrium is shifted dramatically toward open domain conformations. In light of increasing evidence that the stability, in addition to the extent, of domain closure is a critical component of the channel activation mechanism, the differences in domain opening and closing equilibria detected for glutamate and kainate should be useful structural measures for interpreting the markedly different current responses evoked by these agonists.
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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.