Cited by 181Neuroscience and Neuropharmacology ResearchAmino Acid Enzymes and MetabolismReceptor Mechanisms and Signaling

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Identification and Mechanism of Action of Two Histidine Residues Underlying High-Affinity Zn2+ Inhibition of the NMDA Receptor

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Choi, Yun-Beom, Lipton, Stuart A·1999·Neuron

DOI 10.1016/s0896-6273(00)80763-1

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Abstract

Zinc (Zn2+) inhibition of N-methyl-D-aspartate receptor (NMDAR) activity involves both voltage-independent and voltage-dependent components. Recombinant NR1/NR2A and NR1/NR2B receptors exhibit similar voltage-dependent block, but voltage-independent Zn2+ inhibition occurs with much higher affinity for NR1/NR2A than NR1/NR2B receptors (nanomolar versus micromolar IC50, respectively). Here, we show that two neighboring histidine residues on NR2A represent the critical determinant (termed the "short spacer") for high-affinity, voltage-independent Zn2+ inhibition using the Xenopus oocyte expression system and site-directed mutagenesis. Mutation of either one of these two histidine residues (H42 and H44) in the extracellular N-terminal domain of NR2A shifted the IC50 for high-affinity Zn2+ inhibition approximately 200-fold without affecting the EC50 of the coagonists NMDA and glycine. We suggest that the mechanism of high-affinity Zn2+ inhibition on the NMDAR involves enhancement of proton inhibition.

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The biochemical basis of zinc physiology
Vallée, B. L., & Falchuk, K. H. (1993) · Physiological Reviews · doi:10.1152/physrev.1993.73.1.79 · Cited by 3,005
Heteromeric NMDA receptors: molecular and functional distinction of subtypes
Monyer, H., Sprengel, R., Schoepfer, R., Herb, A., Higuchi, M., Lomeli, H., Burnashev, N., Sakmann, B., & Seeburg, P. H. (1992) · Science · doi:10.1126/science.256.5060.1217 · Cited by 2,541
Molecular cloning and characterization of the rat NMDA receptor
Moriyoshi, K., Masu, M., Ishii, T., Shigemoto, R., Mizuno, N., & Nakanishi, S. (1991) · Nature · doi:10.1038/354031a0 · Cited by 1,771
Changing subunit composition of heteromeric NMDA receptors during development of rat cortex
Sheng, M., Cummings, J., Roldan, L. A., Jan, Y. N., & Jan, L. Y. (1994) · Nature · doi:10.1038/368144a0 · Cited by 1,377
Molecular diversity of the NMDA receptor channel
Kutsuwada, T., Kashiwabuchi, N., Mori, H., Sakimura, K., Kushiya, E., Araki, K., Meguro, H., Hisashi, M., Kumanishi, T., Arakawa, M., et al. (1992) · Nature · doi:10.1038/358036a0 · Cited by 1,352
Release of endogenous Zn2+ from brain tissue during activity
Assaf, S. Y., & Chung, S. (1984) · Nature · doi:10.1038/308734a0 · Cited by 1,113
Chemical Modification of Proteins
Roberts, G. C. K. (2012) · Springer eBooks · doi:10.1007/978-3-642-16712-6_100145 · Cited by 1,074
Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs
Liman, E. R., Tytgat, J., & Hess, P. (1992) · Neuron · doi:10.1016/0896-6273(92)90239-a · Cited by 1,072
The Role of Zinc in Selective Neuronal Death After Transient Global Cerebral Ischemia
Koh, J., Suh, S. W., Gwag, B. J., He, Y. Y., Hsu, C. Y., & Choi, D. W. (1996) · Science · doi:10.1126/science.272.5264.1013 · Cited by 1,070
Molecular characterization of the family of the N-methyl-D-aspartate receptor subunits.
Ishii, T. M., Moriyoshi, K., Sugihara, H., Sakurada, K., Kadotani, H., Yokoi, M., Akazawa, C., Shigemoto, R., Mizuno, N., & Masu, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53849-7 · Cited by 980

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Authors: Choi, Y.-B., & Lipton, S. A.
Affiliations: Brigham and Women's Hospital (US)
Corresponding author: Lipton, Stuart A
ORCID: Choi, Yun-Beom
Lipton, Stuart A
Venue: Neuron
Publisher: Elsevier BV
Published: 1999-05
Volume: 23
Issue: 1
Pages: 171-180
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/s0896-6273(00)80763-1
OpenAlex: W1970564284
Cited by: 180
References: 48
Citations by year: 2025: 2 · 2024: 1 · 2022: 4 · 2021: 2 · 2020: 4 · 2019: 3 · 2018: 7 · 2017: 4 · 2016: 8 · 2015: 5 · 2014: 10 · 2013: 4 · 2012: 12
FWCI: 3.71
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5191 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Eye Institute (R01EY005477)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (P01HD029587)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: zinc inhibition, NMDA receptor, NR2A subunit, histidine residues, voltage-dependent block, proton inhibition, site-directed mutagenesis
MeSH terms: Animals, Diethyl Pyrocarbonate, Female, Histidine, Mutation, Oocytes, Xenopus laevis, Zinc, Receptors, N-Methyl-D-Aspartate, Patch-Clamp Techniques, Protein Isoforms

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Identification and Mechanism of Action of Two Histidine Residues Underlying High-Affinity Zn2+ Inhibition of the NMDA Receptor

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