ArticleNature structural & molecular biology2024
Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Postoperative Impairment of GluA2 Ttrafficking in CA3 Induces Memory Consolidation Deficits in Aged Mice by Disrupting SPW-R in CA1.Journal of molecular neuroscience : MN · 2026Article
- Mapping the multi-domain allosteric network for CKAMP44 modulation of AMPA receptors.The Journal of biological chemistry · 2026Article
- Assembly and gating mechanism of native AMPA receptors from the cerebellum.Cell research · 2026Article
- Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.Science (New York, N.Y.) · 2026Article
- Global hotspots and trends in AMPA receptor research (2000-2025): a bibliometric and visualization analysis.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- The Protonic Brain: Nanoscale pH Dynamics, Proton Wires, and Acid-Base Information Coding in Neural Tissue.International journal of molecular sciences · 2026Review
- Studying Synchronization of Neural Oscillators through NMDA-AMPA Receptor interactions.Chaos, solitons, and fractals · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins.Nature structural & molecular biology · 2025Article
- Ultralow-Power Peptide-Based Memristor Enabled by Emulation of Proton-Mediated Synaptic Signaling.Small methods · 2025Article
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- Gating and noelin clustering of native CaNature · 2025Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Article
- AMPA receptor diffusional trapping machinery as an early therapeutic target in neurodegenerative and neuropsychiatric disorders.Translational neurodegeneration · 2025Review
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8 authors.
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Abstract
AMPA glutamate receptors (AMPARs) are ion channel tetramers that mediate the majority of fast excitatory synaptic transmission. They are composed of four subunits (GluA1-GluA4); the GluA2 subunit dominates AMPAR function throughout the forebrain. Its extracellular N-terminal domain (NTD) determines receptor localization at the synapse, ensuring reliable synaptic transmission and plasticity. This synaptic anchoring function requires a compact NTD tier, stabilized by a GluA2-specific NTD interface. Here we show that low pH conditions, which accompany synaptic activity, rupture this interface. All-atom molecular dynamics simulations reveal that protonation of an interfacial histidine residue (H208) centrally contributes to NTD rearrangement. Moreover, in stark contrast to their canonical compact arrangement at neutral pH, GluA2 cryo-electron microscopy structures exhibit a wide spectrum of NTD conformations under acidic conditions. We show that the consequences of this pH-dependent conformational control are twofold: rupture of the NTD tier slows recovery from desensitized states and increases receptor mobility at mouse hippocampal synapses. Therefore, a proton-triggered NTD switch will shape both AMPAR location and kinetics, thereby impacting synaptic signal transmission.
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