ArticleThe EMBO journal2013
CaMKII-dependent phosphorylation of GluK5 mediates plasticity of kainate receptors.
Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Two Signaling Modes Are Better than One: Flux-Independent Signaling by Ionotropic Glutamate Receptors Is Coming of Age.Biomedicines · 2024Review
- Dissecting the contribution of human chromosome 21 syntenic regions to recognition memory processes in adult and aged mouse models of Down syndrome.Frontiers in behavioral neuroscience · 2024Article
- BDNF and Lactate as Modulators of Hippocampal CA3 Network Physiology.Cellular and molecular neurobiology · 2023Review
- Presynaptic Kainate Receptors onto Somatostatin Interneurons Are Recruited by Activity throughout Development and Contribute to Cortical Sensory Adaptation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Activation of Extrasynaptic Kainate Receptors Drives Hilar Mossy Cell Activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Spatial regulation of coordinated excitatory and inhibitory synaptic plasticity at dendritic synapses.Cell reports · 2022Article
- Structure, Function, and Regulation of the Kainate Receptor.Sub-cellular biochemistry · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Sustained postsynaptic kainate receptor activation downregulates AMPA receptor surface expression and induces hippocampal LTD.iScience · 2021Article
- Role of Satb1 and Satb2 Transcription Factors in the Glutamate Receptors Expression and CaInternational journal of molecular sciences · 2021Article
- Kainate Receptor Activation Shapes Short-Term Synaptic Plasticity by Controlling Receptor Lateral Mobility at Glutamatergic Synapses.Cell reports · 2020Article
- Exciting Times: New Advances Towards Understanding the Regulation and Roles of Kainate Receptors.Neurochemical research · 2019Review
- Glutamatergic Signaling in the Central Nervous System: Ionotropic and Metabotropic Receptors in Concert.Neuron · 2018Review
- Molecular mimicking of C-terminal phosphorylation tunes the surface dynamics of CaThe Journal of biological chemistry · 2018Article
- PKC SUMOylation inhibits the binding of 14-3-3τ to GluK2.Channels (Austin, Tex.) · 2017Article
- Cortical kainate receptors and behavioral anxiety.Molecular brain · 2017Review
- Operation and plasticity of hippocampal CA3 circuits: implications for memory encoding.Nature reviews. Neuroscience · 2017Review
- Molecular determinants for the strictly compartmentalized expression of kainate receptors in CA3 pyramidal cells.Nature communications · 2016Article
- P2X-mediated AMPA receptor internalization and synaptic depression is controlled by two CaMKII phosphorylation sites on GluA1 in hippocampal neurons.Scientific reports · 2016Article
- Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor.Cell reports · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calmodulin-dependent kinase II (CaMKII) is key for long-term potentiation of synaptic AMPA receptors. Whether CaMKII is involved in activity-dependent plasticity of other ionotropic glutamate receptors is unknown. We show that repeated pairing of pre- and postsynaptic stimulation at hippocampal mossy fibre synapses induces long-term depression of kainate receptor (KAR)-mediated responses, which depends on Ca(2+) influx, activation of CaMKII, and on the GluK5 subunit of KARs. CaMKII phosphorylation of three residues in the C-terminal domain of GluK5 subunit markedly increases lateral mobility of KARs, possibly by decreasing the binding of GluK5 to PSD-95. CaMKII activation also promotes surface expression of KARs at extrasynaptic sites, but concomitantly decreases its synaptic content. Using a molecular replacement strategy, we demonstrate that the direct phosphorylation of GluK5 by CaMKII is necessary for KAR-LTD. We propose that CaMKII-dependent phosphorylation of GluK5 is responsible for synaptic depression by untrapping of KARs from the PSD and increased diffusion away from synaptic sites.
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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.