ArticleNeuron2016
Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes.
Article in Neuron, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 70 citations in OpenAlex.
- Tunable AMPA receptor function via recurrent evolution of heterotetramers.The Journal of general physiology · 2026Article
- Tuning of AMPA receptor activation by inhibitory auxiliary subunits and epilepsy-associated disease mutations.Nature communications · 2026Article
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- Neuroimmune Dysregulation and AI-Driven Therapeutic Strategies in Alzheimer's Disease.Cellular and molecular neurobiology · 2025Review
- GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins.Nature structural & molecular biology · 2025Article
- Article
- Structure of transmembrane AMPA receptor regulatory protein subunit γ2.Nature communications · 2025Article
- The open gate of the AMPA receptor forms a CaNature structural & molecular biology · 2024Article
- Exploring the impact of the stargazin V143L mutation on the dynamics of the AMPA receptor: stargazin complex.Frontiers in cellular neuroscience · 2024Article
- GSG1L-containing AMPA receptor complexes are defined by their spatiotemporal expression, native interactome and allosteric sites.Nature communications · 2023Article
- Article
- Alternative Splicing of the Flip/Flop Cassette and TARP Auxiliary Subunits Engage in a Privileged Relationship That Fine-Tunes AMPA Receptor Gating.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Protein-Protein Interaction Studies Using Molecular Dynamics Simulation.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Structural insights into function of ionotropic glutamate receptors.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022Article
- The action of Con-ikot-ikot toxin on single AMPA-type glutamate receptors.The Journal of general physiology · 2022Article
- Mechanisms underlying TARP modulation of the GluA1/2-γ8 AMPA receptor.Nature communications · 2022Article
- Structure and desensitization of AMPA receptor complexes with type II TARP γ5 and GSG1L.Molecular cell · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Neurotransmitter-gated ion channels adopt different gating modes to fine-tune signaling at central synapses. At glutamatergic synapses, high and low activity of AMPA receptors (AMPARs) is observed when pore-forming subunits coassemble with or without auxiliary subunits, respectively. Whether a common structural pathway accounts for these different gating modes is unclear. Here, we identify two structural motifs that determine the time course of AMPAR channel activation. A network of electrostatic interactions at the apex of the AMPAR ligand-binding domain (LBD) is essential for gating by pore-forming subunits, whereas a conserved motif on the lower, D2 lobe of the LBD prolongs channel activity when auxiliary subunits are present. Accordingly, channel activity is almost entirely abolished by elimination of the electrostatic network but restored via auxiliary protein interactions at the D2 lobe. In summary, we propose that activation of native AMPAR complexes is coordinated by distinct structural pathways, favored by the association/dissociation of auxiliary subunits.
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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.