ArticleeLife2018
Auxiliary subunits keep AMPA receptors compact during activation and desensitization.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Mapping the multi-domain allosteric network for CKAMP44 modulation of AMPA receptors.The Journal of biological chemistry · 2026Article
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 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
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- A mechanism of CALHM1 ion channel gating.American journal of physiology. Cell physiology · 2025Article
- Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.Nature structural & molecular biology · 2024Article
- Structural dynamics in α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor gating.Current opinion in structural biology · 2024Review
- Activity-dependent diffusion trapping of AMPA receptors as a key step for expression of early LTP.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Tuning synaptic strength by regulation of AMPA glutamate receptor localization.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- Article
- The action of Con-ikot-ikot toxin on single AMPA-type glutamate receptors.The Journal of general physiology · 2022Article
- Delta glutamate receptors are functional glycine- and ᴅ-serine-gated cation channels in situ.Science advances · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Measurements of the Timescale and Conformational Space of AMPA Receptor Desensitization.Biophysical journal · 2020Article
- Mechanism of modulation of AMPA receptors by TARP-γ8.The Journal of general physiology · 2020Article
- Structural and functional insights into transmembrane AMPA receptor regulatory protein complexes.The Journal of general physiology · 2019Review
- Structure and mechanism of AMPA receptor - auxiliary protein complexes.Current opinion in structural biology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Signal transduction at vertebrate excitatory synapses involves the rapid activation of AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionate) receptors, glutamate-gated ion channels whose four subunits assemble as a dimer-of-dimers. Technical advances in cryo-electron microscopy brought a slew of full-length structures of AMPA receptors, on their own and in combination with auxiliary subunits. These structures indicate that dimers might undergo substantial lateral motions during gating, opening up the extracellular layer along the central twofold symmetry axis. We used bifunctional methanethiosulfonate cross-linkers to calibrate the conformations found in functional AMPA receptors in the presence and absence of the auxiliary subunit Stargazin. Our data indicate that extracellular layer of AMPA receptors can get trapped in stable, opened-up conformations, especially upon long exposures to glutamate. In contrast, Stargazin limits this conformational flexibility. Thus, under synaptic conditions, where brief glutamate exposures and the presence of auxiliary proteins dominate, extracellular domains of AMPA receptors likely stay compact during gating.
Indexed as
Identifiers
What OpenQuestion holds
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.