ArticleBiophysical journal1996
Kinetics of homomeric GluR6 glutamate receptor channels.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 95 citations in OpenAlex.
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Article
- Structural and compositional diversity in the kainate receptor family.Cell reports · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Subunit-selective iGluR antagonists can potentiate heteromeric receptor responses by blocking desensitization.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Zinc Modulates Olfactory Bulb Kainate Receptors.Neuroscience · 2020Article
- Kainate Receptors Play a Role in Modulating Synaptic Transmission in the Olfactory Bulb.Neuroscience · 2018Article
- The auxiliary subunits Neto1 and Neto2 have distinct, subunit-dependent effects at recombinant GluK1- and GluK2-containing kainate receptors.Neuropharmacology · 2015Article
- Contributions of different kainate receptor subunits to the properties of recombinant homomeric and heteromeric receptors.Neuroscience · 2014Article
- The neurotoxin domoate causes long-lasting inhibition of the kainate receptor GluK5 subunit.Neuropharmacology · 2014Article
- Kainate receptor subunit diversity underlying response diversity in retinal off bipolar cells.The Journal of physiology · 2014Article
- Tethered ligands reveal glutamate receptor desensitization depends on subunit occupancy.Nature chemical biology · 2014Article
- Modulation of homomeric and heteromeric kainate receptors by the auxiliary subunit Neto1.The Journal of physiology · 2013Article
- Modulation of GluK2a subunit-containing kainate receptors by 14-3-3 proteins.The Journal of biological chemistry · 2013Article
- Crosslinking the ligand-binding domain dimer interface locks kainate receptors out of the main open state.The Journal of physiology · 2013Article
- Dancing partners at the synapse: auxiliary subunits that shape kainate receptor function.Nature reviews. Neuroscience · 2012Review
- Channel-opening kinetic mechanism of wild-type GluK1 kainate receptors and a C-terminal mutant.Biochemistry · 2012Article
- Distinct functional roles of subunits within the heteromeric kainate receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Distinct functions of kainate receptors in the brain are determined by the auxiliary subunit Neto1.Nature neuroscience · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied the kinetics of the unedited version of rat GluR6 glutamate (glu) receptor channels, GluR6Q, in outside-out patches using a system for submillisecond solution exchange. Half-maximum activation of the channels was reached with approximately 0.5 microM glu. The maximum slope of the double-logarithmic plot of the peak current versus glu was approximately 1.3, indicating that at least two binding steps are necessary to open the channels. Currents in response to a pulse of 10 microM glu had a short rise time (10-90% of peak current) of approximately 220 microseconds at approximately 20 degrees C. The rise time increased with falling glu concentration, reaching approximately 6.0 ms with 10 microM glu. In the continued presence of glu, the channels desensitized, and this desensitization can be described with a single time constant of approximately 7.0 ms for a pulse of 10 microM glu. The steady-state current in response to a long pulse of 10 microM glu was below 1/280th of the peak current. The time constant of desensitization was found to be independent of concentration between 30.0 and 0.3 microM glu, but to be increased for lower concentrations. After a short pulse of 1 ms duration and 10 or 0.3 microM glu, currents decayed with a time constant of approximately 2.5 ms. Recovery from desensitization after a pulse took approximately 5 s, and the half-time of recovery was approximately 2.2 s. Continuous application of low concentrations of glutamate reduced the peak currents in response to a pulse of 10 microM glu markedly. Fifty percent response reduction was observed in the continuous presence of approximately 0.3 microM glu. Our results for homomeric GluR6 agree with a cyclical reaction scheme developed for completely desensitizing, glu-activated channels on crayfish muscles.
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