ArticleBiophysical journal2001
High-affinity Zn block in recombinant N-methyl-D-aspartate receptors with cysteine substitutions at the Q/R/N site.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- Article
- The Role of Zinc in Modulating Acid-Sensing Ion Channel Function.Biomolecules · 2023Review
- Involvement of NR2A- or NR2B-containing N-methyl-D-aspartate receptors in the potentiation of cortical layer 5 pyramidal neurone inputs depends on the developmental stage.The European journal of neuroscience · 2007Article
- Differential regulation of ionotropic glutamate receptors.Biophysical journal · 2007Article
- NR3A modulates the outer vestibule of the "NMDA" receptor channel.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- ASIC1a-specific modulation of acid-sensing ion channels in mouse cortical neurons by redox reagents.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Subunit-dependent high-affinity zinc inhibition of acid-sensing ion channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- Staggering of subunits in NMDAR channels.Biophysical journal · 2002Article
- Modulation by permeant ions of Mg(2+) inhibition of NMDA-activated whole-cell currents in rat cortical neurons.The Journal of physiology · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In ionotropic glutamate receptors, many channel properties (e.g., selectivity, ion permeation, and ion block) depend on the residue (glutamine, arginine, or asparagine) located at the tip of the pore loop (the Q/R/N site). We substituted a cysteine for the asparagine present at that position in both NR1 and NR2 N-methyl-D-aspartate (NMDA) receptor subunits. Under control conditions, receptors containing mutated NR1 and NR2 subunits show much smaller glutamate responses than wild-type receptors. However, this difference disappears upon addition of heavy metal chelators in the extracellular bath. The presence of cysteines at the Q/R/N site in both subunits of NR1/NR2C receptors results in a 220,000-fold increase in sensitivity of the inhibition by extracellular Zn. In contrast with the high-affinity Zn inhibition of wild-type NR1/NR2A receptors, the high-affinity Zn inhibition of mutated NR1/NR2C receptors shows a voltage dependence, which resembles very much that of the block by extracellular Mg. This indicates that the Zn inhibition of the mutated receptors results from a channel block involving Zn binding to the thiol groups introduced into the selectivity filter. Taking advantage of the slow kinetics of the Zn block, we show that both blocking and unblocking reactions require prior opening of the channel.
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