ArticleThe Journal of biological chemistry2013
Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Cryo-EM structures of apo, agonist- and antagonist-bound heteromeric kainate receptors.Science advances · 2026Article
- Neto2 Phosphorylation Promotes Neuronal Loss in KA-Induced Epileptic Rat Hippocampus by Upregulating the Interaction with GluK2.Neurochemical research · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- Glutamate, Gangliosides, and the Synapse: Electrostatics at Work in the Brain.International journal of molecular sciences · 2024Review
- Coordinated interplay between palmitoylation, phosphorylation and SUMOylation regulates kainate receptor surface expression.Frontiers in molecular neuroscience · 2023Article
- Sustained postsynaptic kainate receptor activation downregulates AMPA receptor surface expression and induces hippocampal LTD.iScience · 2021Article
- 4.1N-Mediated Interactions and Functions in Nerve System and Cancer.Frontiers in molecular biosciences · 2021Review
- Role of actin cytoskeleton in the organization and function of ionotropic glutamate receptors.Current research in structural biology · 2021Review
- A novel role for the late-onset Alzheimer's disease (LOAD)-associated protein Bin1 in regulating postsynaptic trafficking and glutamatergic signaling.Molecular psychiatry · 2020Article
- The Kainate Receptor Subunit GluK2 Interacts With KCC2 to Promote Maturation of Dendritic Spines.Frontiers in cellular neuroscience · 2020Article
- The glutamate receptor GluK2 contributes to the regulation of glucose homeostasis and its deterioration during aging.Molecular metabolism · 2019Article
- Exciting Times: New Advances Towards Understanding the Regulation and Roles of Kainate Receptors.Neurochemical research · 2019Review
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- Insights Into ProteinFrontiers in molecular neuroscience · 2018Review
- Palmitoylation as a Functional Regulator of Neurotransmitter Receptors.Neural plasticity · 2018Review
- Synaptic homeostasis requires the membrane-proximal carboxy tail of GluA2.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Assembly, Secretory Pathway Trafficking, and Surface Delivery of Kainate Receptors Is Regulated by Neuronal Activity.Cell reports · 2017Article
- Molecular determinants for the strictly compartmentalized expression of kainate receptors in CA3 pyramidal cells.Nature communications · 2016Article
- A proteomic analysis reveals the interaction of GluK1 ionotropic kainate receptor subunits with Go proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- The Cell Adhesion Molecule Necl-4/CADM4 Serves as a Novel Regulator for Contact Inhibition of Cell Movement and Proliferation.PloS one · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Kainate receptors exhibit a highly compartmentalized distribution within the brain; however, the molecular and cellular mechanisms that coordinate their expression at neuronal sites of action are poorly characterized. Here we report that the GluK1 and GluK2 kainate receptor subunits interact with the spectrin-actin binding scaffolding protein 4.1N through a membrane-proximal domain in the C-terminal tail. We found that this interaction is important for the forward trafficking of GluK2a receptors, their distribution in the neuronal plasma membrane, and regulation of receptor endocytosis. The association between GluK2a receptors and 4.1N was regulated by both palmitoylation and protein kinase C (PKC) phosphorylation of the receptor subunit. Palmitoylation of the GluK2a subunit promoted 4.1N association, and palmitoylation-deficient receptors exhibited reduced neuronal surface expression and compromised endocytosis. Conversely, PKC activation decreased 4.1N interaction with GluK2/3-containing kainate receptors in acute brain slices, an effect that was reversed after inhibition of PKC. Our data and previous studies therefore demonstrate that these two post-translational modifications have opposing effects on 4.1N association with GluK2 kainate and GluA1 AMPA receptors. The convergence of the signaling pathways regulating 4.1N protein association could thus result in the selective removal of AMPA receptors from the plasma membrane while simultaneously promoting the insertion and stabilization of kainate receptors, which may be important for tuning neuronal excitability and synaptic plasticity.
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