ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
Permeant ion effects on external Mg2+ block of NR1/2D NMDA receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
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- Glutamate spillover drives robust all-or-none dendritic plateau potentials-anFrontiers in cellular neuroscience · 2023Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Magnesium Acts as a Second Messenger in the Regulation of NMDA Receptor-Mediated CREB Signaling in Neurons.Molecular neurobiology · 2020Article
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
- NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017Article
- The discovery of human of GLUD2 glutamate dehydrogenase and its implications for cell function in health and disease.Neurochemical research · 2014Review
- Astrocytes convert network excitation to tonic inhibition of neurons.BMC biology · 2012Article
- A single GluN2 subunit residue controls NMDA receptor channel properties via intersubunit interaction.Nature neuroscience · 2012Article
- Neuregulin1/ErbB4-induced migration in ST14A striatal progenitors: calcium-dependent mechanisms and modulation by NMDA receptor activation.BMC neuroscience · 2011Article
- Distinct pharmacological and functional properties of NMDA receptors in mouse cortical astrocytes.British journal of pharmacology · 2011Article
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Stoichiometry of N-methyl-D-aspartate receptors within the suprachiasmatic nucleus.Journal of neurophysiology · 2010Article
- Ionic flow enhances low-affinity binding: a revised mechanistic view into Mg2+ block of NMDA receptors.The Journal of physiology · 2010Article
- Mg2+ imparts NMDA receptor subtype selectivity to the Alzheimer's drug memantine.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Voltage-dependent gating of NR1/2B NMDA receptors.The Journal of physiology · 2008Article
- NR2B- and NR2D-containing synaptic NMDA receptors in developing rat substantia nigra pars compacta dopaminergic neurones.The Journal of physiology · 2008Article
- Mg2+ and memantine block of rat recombinant NMDA receptors containing chimeric NR2A/2D subunits expressed in Xenopus laevis oocytes.The Journal of physiology · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-dependent channel block by external Mg2+ (Mg2+(o)) of NMDA receptors is an essential determinant of synaptic function. The resulting Mg2+(o) inhibition of NMDA responses depends strongly on receptor subunit composition: NR1/2A and NR1/2B receptors are more strongly inhibited by Mg2+(o) than are NR1/2C or NR1/2D receptors. Previous work showed that permeant ions have profound effects on Mg2+(o) block of NMDA receptors composed of NR1, NR2A, and NR2B subunits. Whether permeant ions affect Mg2+(o) inhibition of NR1/2C or NR1/2D receptors is unknown. We investigated the effects of permeant ions on Mg2+(o) block of NR1/2D receptors by integrating results from whole-cell recordings, single-channel recordings, and kinetic modeling. Lowering internal [Cs+] caused a voltage-dependent decrease in the Mg2+(o) IC50 and in the apparent Mg2+(o) unblocking rate, and increase in the apparent Mg2+(o) blocking rate (k(+,app)) of NR1/2D receptors. Lowering external [Na+] caused modest voltage-dependent changes in the Mg2+(o) IC50 and k(+,app). These data can be explained by a kinetic model in which occupation of either of two external permeant ion binding sites prevents Mg2+(o) entry into the channel. Occupation of an internal permeant ion binding site prevents Mg2+(o) permeation and accelerates Mg2+(o) unblock to the external solution. We conclude that variations in permeant ion site properties shape the NR2 subunit dependence of Mg2+(o) block. Furthermore, the external channel entrance varies little among NMDA receptor subtypes. Differences in the Mg2+(o) blocking site, and particularly in the selectivity filter and internal channel entrance, are principally responsible for the subunit dependence of Mg2+(o) block.
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