ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012
The auxiliary subunits Neto1 and Neto2 reduce voltage-dependent inhibition of recombinant kainate receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 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
- Multilayered regulation of GluK3 kainate receptors is mediated by Neto subunits and zinc.Communications biology · 2026Article
- Multilayer control of KaiR1D-autoreceptor function by the auxiliary protein Neto.bioRxiv : the preprint server for biology · 2025Article
- Intracellular Spermine Is a Key Player in GSG1L's Regulation of Calcium-Permeable AMPAR Channel Conductance and Recovery from Desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
- Article
- Enhanced functional detection of synaptic calcium-permeable AMPA receptors using intracellular NASPM.eLife · 2023Article
- Structure, Function, and Regulation of the Kainate Receptor.Sub-cellular biochemistry · 2022Review
- Kainate receptor modulation by NETO2.Nature · 2021Article
- 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
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites.The Journal of biological chemistry · 2019Article
- Polyamine-mediated channel block of ionotropic glutamate receptors and its regulation by auxiliary proteins.The Journal of biological chemistry · 2018Review
- Kainate Receptors Play a Role in Modulating Synaptic Transmission in the Olfactory Bulb.Neuroscience · 2018Article
- Ion permeation in ionotropic glutamate receptors: Still dynamic after all these years.Current opinion in physiology · 2018Article
- Stargazin and cornichon-3 relieve polyamine block of AMPA receptors by enhancing blocker permeation.The Journal of general physiology · 2018Article
- Phosphorylation of the kainate receptor (KAR) auxiliary subunit Neto2 at serine 409 regulates synaptic targeting of the KAR subunit GluK1.The Journal of biological chemistry · 2017Article
- Neto Auxiliary Subunits Regulate Interneuron Somatodendritic and Presynaptic Kainate Receptors to Control Network Inhibition.Cell reports · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kainate receptors can be subject to voltage-dependent block by intracellular polyamines, which causes inward rectification of the current-voltage relationship. Sensitivity to polyamine block is largely determined by the identity of a residue within the pore domain that can be altered through RNA editing. This process causes replacement of the encoded glutamine(Q) with a positively charged arginine(R), eliminating polyamine inhibition and thus inward rectification. In neurons, kainate receptors can associate with the auxiliary subunits Neto1 or Neto2. These transmembrane proteins alter the trafficking, channel kinetics, and pharmacology of the receptors in a subunit-dependent manner. We found that coexpression of Neto subunits with recombinant GluK2(Q) kainate receptors greatly reduced inward rectification without altering calcium permeability. This effect was separate from modulation of channel kinetics, as mutations within the extracellular LDLa domain of the Neto proteins completely eliminated their effects on desensitization but only reduced their effects on rectification. Conversely, deletion of the intracellular C-terminal domain of Neto1 or Neto2 or neutralization of positively charged residues within this domain prevented the reduction in rectification but did not alter effects on channel kinetics. These results demonstrate new roles for Neto1 and Neto2 in regulating kainate receptor function and identify domains within these auxiliary subunits important for mediating their effects.
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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.