ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005
Q/R site editing controls kainate receptor inhibition by membrane fatty acids.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
- Trapping of spermine, Kukoamine A, and polyamine toxin blockers in GluK2 kainate receptor channels.Nature communications · 2024Article
- Kainate Receptor Antagonists: Recent Advances and Therapeutic Perspective.International journal of molecular sciences · 2023Review
- RNA editing of ion channels and receptors in physiology and neurological disorders.Oxford open neuroscience · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Interplay between Gating and Block of Ligand-Gated Ion Channels.Brain sciences · 2020Review
- Cadmium activates AMPA and NMDA receptors with M3 helix cysteine substitutions.The Journal of general physiology · 2020Article
- Homomeric GluA2(R) AMPA receptors can conduct when desensitized.Nature communications · 2019Article
- Architecture of the heteromeric GluA1/2 AMPA receptor in complex with the auxiliary subunit TARP γ8.Science (New York, N.Y.) · 2019Article
- Cadmium opens GluK2 kainate receptors with cysteine substitutions at the M3 helix bundle crossing.The Journal of general physiology · 2019Article
- The Good and the Bad of Glutamate Receptor RNA Editing.Molecular neurobiology · 2017Review
- Chimeric Glutamate Receptor Subunits Reveal the Transmembrane Domain Is Sufficient for NMDA Receptor Pore Properties but Some Positive Allosteric Modulators Require Additional Domains.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Glutamate receptor pores.The Journal of physiology · 2015Review
- Regulation of Ion Channel and Transporter Function Through RNA Editing.Current issues in molecular biology · 2015Review
- Radial symmetry in a chimeric glutamate receptor pore.Nature communications · 2014Article
- Q/R site interactions with the M3 helix in GluK2 kainate receptor channels revealed by thermodynamic mutant cycles.The Journal of general physiology · 2013Article
- (n-3) fatty acids and cardiovascular health: are effects of EPA and DHA shared or complementary?The Journal of nutrition · 2012Review
- Coactivation of thalamic and cortical pathways induces input timing-dependent plasticity in amygdala.Nature neuroscience · 2011Article
- An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.The Journal of biological chemistry · 2011Article
- Fatty acid modulation and polyamine block of GluK2 kainate receptors analyzed by scanning mutagenesis.The Journal of general physiology · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RNA editing within the pore loop controls the pharmacology and permeation properties of ion channels formed by neuronal AMPA and kainate receptor subunits. Genomic sequences for the glutamate receptor 2 (GluR2) subunit of AMPA receptors and the GluR5 and GluR6 subunits of kainate receptors all encode a neutral glutamine (Q) residue within the channel pore that can be converted by RNA editing to a positively charged arginine (R). Receptors comprised of unedited subunits are permeable to calcium and display inwardly rectifying current-voltage relationships, because of blocking of outward current by intracellular polyamines. In contrast, receptors that include edited subunits conduct less calcium, resist polyamine block, and have relatively linear current-voltage relationships. We showed previously that cis-unsaturated fatty acids, including arachidonic acid and docosahexanoic acid, exert a potent block of native kainate receptors as well as homomeric recombinant receptors formed by transfection of heterologous cells with cDNA for the GluR6(R) subunit. Here, we show that fatty acid blockade of recombinant homomeric and heteromeric kainate receptors is strongly dependent on editing at the Q/R site. Recombinant channels that include unedited subunits exhibit significantly weaker block than channels made up of fully edited subunits. Inhibition of fully edited channels is equivalent at voltages from -70 to +40 mV and is noncompetitive, consistent with allosteric regulation of channel function.
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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.