ReviewThe Journal of physiology2010
Ion-dependent gating of kainate receptors.
Review in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- Cryo-EM structures of apo, agonist- and antagonist-bound heteromeric kainate receptors.Science advances · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Shared and unique aspects of ligand- and voltage-gated ion-channel gating.The Journal of physiology · 2018Article
- Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes.Neuron · 2016Article
- Identification of critical functional determinants of kainate receptor modulation by auxiliary protein Neto2.The Journal of physiology · 2015Article
- Retour aux sources: defining the structural basis of glutamate receptor activation.The Journal of physiology · 2015Review
- Ionotropic glutamate receptors: alive and kicking.The Journal of physiology · 2015Article
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
- The multifaceted subunit interfaces of ionotropic glutamate receptors.The Journal of physiology · 2015Review
- The Concise Guide to PHARMACOLOGY 2013/14: ligand-gated ion channels.British journal of pharmacology · 2013Article
- Defining the structural relationship between kainate-receptor deactivation and desensitization.Nature structural & molecular biology · 2013Article
- Zinc potentiates GluK3 glutamate receptor function by stabilizing the ligand binding domain dimer interface.Neuron · 2012Article
- Dancing partners at the synapse: auxiliary subunits that shape kainate receptor function.Nature reviews. Neuroscience · 2012Review
- Kainate receptors coming of age: milestones of two decades of research.Trends in neurosciences · 2011Review
- Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Cations but not anions regulate the responsiveness of kainate receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ligand-gated ion channels are an important class of signalling protein that depend on small chemical neurotransmitters such as acetylcholine, l-glutamate, glycine and gamma-aminobutyrate for activation. Although numerous in number, neurotransmitter substances have always been thought to drive the receptor complex into the open state in much the same way and not rely substantially on other factors. However, recent work on kainate-type (KAR) ionotropic glutamate receptors (iGluRs) has identified an exception to this rule. Here, the activation process fails to occur unless external monovalent anions and cations are present. This absolute requirement of ions singles out KARs from all other ligand-gated ion channels, including closely related AMPA- and NMDA-type iGluR family members. The uniqueness of ion-dependent gating has earmarked this feature of KARs as a putative target for the development of selective ligands; a prospect all the more compelling with the recent elucidation of distinct anion and cation binding pockets. Despite these advances, much remains to be resolved. For example, it is still not clear how ion effects on KARs impacts glutamatergic transmission. I conclude by speculating that further analysis of ion-dependent gating may provide clues into how functionally diverse iGluRs families emerged by evolution. Consequently, ion-dependent gating of KARs looks set to continue to be a subject of topical inquiry well into the future.
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What OpenQuestion holds
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.