ArticleNature communications2025
Structural insights into kainate receptor desensitization.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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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.
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Who cites it
7 citing papers in PubMed.
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- Cryo-EM structures of apo, agonist- and antagonist-bound heteromeric kainate receptors.Science advances · 2026Article
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- Auxiliary subunits reshape structural asymmetry and functional plasticity in heterotetrameric GluA1/A2 AMPA receptor core.Nature communications · 2026Article
- Multilayered regulation of GluK3 kainate receptors is mediated by Neto subunits and zinc.Communications biology · 2026Article
- Activation of kainate receptor GluK2-Neto2 complex.Nature structural & molecular biology · 2025Article
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
Corrections and comments
- Update of
Authors and funding
3 authors.
Funding
Abstract
Kainate receptors (KARs) belong to the ionotropic glutamate receptor (iGluR) family and play critical roles in mediating excitatory neurotransmission and regulating neurotransmitter release. Receptor desensitization is a critical factor for regulating the strength of synaptic transmission. Notwithstanding their overall structural similarity to AMPA receptors, KARs exhibit a desensitized conformation that is distinct from that of most other iGluRs. Despite extensive studies on KARs, a fundamental question remains unresolved: why do KARs require large conformational changes upon desensitization? Here we show cryo-electron microscopy structures of GluK2 containing double cysteine mutations, captured in non-active and various desensitized conformations. In the shallow-desensitized conformation, two cysteine crosslinks stabilize the receptors in a conformation resembling the typical desensitized state of non-KAR iGluRs. Our patch-clamp recordings and fluctuation analysis suggest that KARs in the shallow-desensitized state remain ion-permeable. This finding indicates that the lateral rotational movement of the KAR ligand-binding domains is critical for complete channel closure and stabilization of the fully desensitized receptor. Overall, this study elucidates the mechanism and conformational dynamics of KARs during desensitization.
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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 Socratic graph.