ArticleFrontiers in molecular neuroscience2012
The essential role of AMPA receptor GluR2 subunit RNA editing in the normal and diseased brain.
Article in Frontiers in molecular neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.
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Who cites it
127 citing papers in PubMed.
- Article
- Article
- AMPA receptor modulation in depression: from molecular mechanisms of plasticity to therapeutic translation.Pharmacological reports : PR · 2026Review
- ADAR-mediated RNA editing in CNS disorders: from pathogenic mechanisms to therapeutic opportunities.Cellular & molecular biology letters · 2026Review
- Environmental Factors Drive Neurodegenerative Diseases Through Glutamate Excitotoxicity: A Convergent Mechanistic Pathway.Neuroscience bulletin · 2026Review
- Assembly and gating mechanism of native AMPA receptors from the cerebellum.Cell research · 2026Article
- In Vivo CRISPR Screening Identifies the Glutamate Receptor GRIA2 as Promoting Peritoneal Metastasis of Gastric Cancer via Calcium-Dependent β-Catenin Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Development of a High-Sensitivity Electrochemical Biosensor for Domoic Acid and Its Cellular Impact on Human Stem and Neuron-Like Cells.Food science & nutrition · 2026Article
- Synergistic antitumor effect of temozolomide and perampanel in pediatric glioma: a case report and in vitro validation using patient-derived glioma sphere cells.Acta neuropathologica communications · 2026Article
- Paradoxical Expression of Ionotropic Glutamate Receptors in Leucocytes.Clinical reviews in allergy & immunology · 2026Article
- Investigating the pathogenic role of calpain proteases and the therapeutic potential of their inhibition in mice modelling Machado-Joseph disease.Human molecular genetics · 2026Article
- Deaminase Modulation Driving a New Era in Drug Development.International journal of molecular sciences · 2025Review
- Interplay Among Synaptic Glutamate Release and Excitotoxicity: Neuronal Damage and Graphene-Based Materials Related Protection.Life (Basel, Switzerland) · 2025Review
- Alternate RNA decoding results in stable and abundant proteins in mammals.bioRxiv : the preprint server for biology · 2025Article
- Simultaneous RNA Sequencing and DNA Methylation Profiling Reveals Neural Mechanisms That Regulate Sensitive Period Behavioral Learning.Genes, brain, and behavior · 2025Article
- ADAR2-mediated Q/R editing of GluA2 in homeostatic synaptic plasticity.Science signaling · 2025Article
- Computer-Aided Discovery of Natural Compounds Targeting the ADAR2 dsRBD2-RNA Interface and Computational Modeling of Full-Length ADAR2 Protein Structure.International journal of molecular sciences · 2025Article
- The Frmpd3 Protein Regulates Susceptibility to Epilepsy by Combining with GRIP and GluA2.Current issues in molecular biology · 2025Article
- Fucoxanthin Inhibits the NMDA and AMPA Receptors Through Regulating the Calcium Response on Substantia Gelatinosa Neurons of the Trigeminal Subnucleus Caudalis in Juvenile Mice.Neural plasticity · 2025Article
- Effects of the AMPAR Antagonist, Perampanel, on Cognitive Function in Rats Exposed to Neonatal Iron Overload.Molecular neurobiology · 2024Article
67 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors are comprised of different combinations of GluA1-GluA4 (also known asGluR1-GluR4 and GluR-A to GluR-D) subunits. The GluA2 subunit is subject to RNA editing by the ADAR2 enzyme, which converts a codon for glutamine (Gln; Q), present in the GluA2 gene, to a codon for arginine (Arg; R) found in the mRNA. AMPA receptors are calcium (Ca(2+))-permeable if they contain the unedited GluA2(Q) subunit or if they lack the GluA2 subunit. While most AMPA receptors in the brain contain the edited GluA2(R) subunit and are therefore Ca(2+)-impermeable, recent evidence suggests that Ca(2+)-permeable AMPA receptors are important in synaptic plasticity, learning, and disease. Strong evidence supports the notion that Ca(2+)-permeable AMPA receptors are usually GluA2-lacking AMPA receptors, with little evidence to date for a significant role of unedited GluA2 in normal brain function. However, recent detailed studies suggest that Ca(2+)-permeable AMPA receptors containing unedited GluA2 do in fact occur in neurons and can contribute to excitotoxic cell loss, even where it was previously thought that there was no unedited GluA2.This review provides an update on the role of GluA2 RNA editing in the healthy and diseased brain and summarizes recent insights into the mechanisms that control this process. We suggest that further studies of the role of unedited GluA2 in normal brain function and disease are warranted, and that GluA2 editing should be considered as a possible contributing factor when Ca(2+)-permeable AMPA receptors are observed.
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