ArticleBiophysical journal2007
Differential regulation of ionotropic glutamate receptors.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- TwoeLife · 2021Article
- The Metallome as a Link Between the "Omes" in Autism Spectrum Disorders.Frontiers in molecular neuroscience · 2021Review
- Calcium-engaged Mechanisms of Nongenomic Action of Neurosteroids.Current neuropharmacology · 2017Review
- Effects of Ketamine on Neuronal Spontaneous Excitatory Postsynaptic Currents and Miniature Excitatory Postsynaptic Currents in the Somatosensory Cortex of Rats.Iranian journal of medical sciences · 2016Article
- Molecular basis of positive allosteric modulation of GluN2B NMDA receptors by polyamines.The EMBO journal · 2011Article
- Zinc and neurogenesis: making new neurons from development to adulthood.Advances in nutrition (Bethesda, Md.) · 2011Review
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Energy transfer ligands of the GluR2 ligand binding core.Biochemistry · 2010Article
- Of mice, rats and men: Revisiting the quinolinic acid hypothesis of Huntington's disease.Progress in neurobiology · 2010Review
- Article
- Supralinear potentiation of NR1/NR3A excitatory glycine receptors by Zn2+ and NR1 antagonist.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Domoic acid toxicologic pathology: a review.Marine drugs · 2008Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ionotropic glutamate receptors (iGluRs), a family of ligand-gated ion channels, are responsible for the majority of fast excitatory neurotransmission in the central nervous system. Within this family, different members serve distinct roles at glutamatergic synapses. Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors mediate fast depolarization while N-methyl-D-aspartate (NMDA) receptors mediate the slower component of the excitatory postsynaptic potential. These disparate functions suggest alternate modes of regulation. In this work, we show that endogenous regulators of iGluRs have different abilities to bind to specific domains of NMDA NR1-1b and AMPA GluR2 subunits. We have previously shown that the sulfated neurosteroids pregnenolone sulfate and 3alpha-hydroxy-5beta-pregnan-20-one sulfate bind to the extracellular glutamate-binding core (S1S2) of the GluR2 subunit. Here we show that neither neurosteroid binds to the S1S2 domain of the NMDA NR1-1b subunit. This NR1-1b NMDA domain does, however, bind to the endogenous polyamines spermine and spermidine as well as Zn(II). Binding of the polyamines and Zn(II) to the S1S2 domain of the GluR2 subunit was not observed. This binding of Zn(II) and polyamines to the S1S2 domain of the NR1-1b subunit defines a new binding site for each of these modulators.
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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.