Gating and permeation of kainate receptors: differences unveiled
Abstract
Kainate receptors (KARs) represent, together with α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) and N-methyl D-aspartate (NMDA) receptors, one of the three families of ionotropic glutamate receptors. Recent advances in the study of their biophysical properties have revealed a surprising diversity. KAR-mediated excitatory postsynaptic currents (EPSCs) are often much slower than AMPA receptor-mediated EPSCs, and this is probably due to the slow deactivation rate of KARs containing the GluK4 or GluK5 subunits. By contrast, GluK3-containing receptors, unlike other AMPA/kainate receptors, desensitize faster at low agonist concentrations, making these receptors insensitive to glutamate spillover from neighboring synapses. Moreover, KARs have a wide range of sensitivities to intracellular polyamines and consequently of voltage dependent activation. Finally, newly discovered associated proteins, such as Neto1 and 2, have marked effects on receptor properties, increasing further the potential diversity of KAR functional properties. Altogether, this functional diversity of KARs could have profound consequences on their ability to shape synaptic transmission under physiological and pathological conditions.
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Even within receptor families, specific subunits and combinations of them or splice variants can have diametrically opposing functional properties from others that are nominally similar.
“Even within receptor families, specific subunits (and combinations of them) or splice variants can have diametrically opposing functional properties from others that are nominally similar (Bettler and Mulle, 1995;Perrais et al., 2010).”
From Glutamate receptors in domestication and modern human evolution (2020) · cites this paper as Perrais et al., 2010
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Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
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- Authors
- Perrais, D., Veran, J., & Mulle, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Perrais, David
- Mulle, Christophe
- Venue
- Trends in Pharmacological Sciences
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 31
- Issue
- 11
- Pages
- 516-522
- ISSN
- 0165-6147 (ISSN-L)
- OpenAlex
- W2083567601
- Cited by
- 67
- References
- 63
- Citations by year
- 2025: 4 · 2023: 2 · 2021: 9 · 2020: 3 · 2019: 7 · 2018: 4 · 2017: 4 · 2016: 3 · 2015: 5 · 2014: 6 · 2013: 4 · 2012: 10
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Pharmacological Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Centre National de la Recherche Scientifique
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- kainate receptors, ionotropic glutamate receptors, receptor gating, ion permeation, receptor desensitization, glutamate spillover, voltage dependence of activation, Neto1, NETO2, excitatory postsynaptic currents, synaptic transmission
- MeSH terms
- Calcium, Humans, Synaptic Transmission, Neurons, Spermine, Synapses, Signal Transduction, Ion Channel Gating, Receptors, N-Methyl-D-Aspartate, Receptors, AMPA, Kainic Acid Receptors, alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid, Glutamic Acid, Excitatory Postsynaptic Potentials, Receptors, Ionotropic Glutamate
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