ArticleeLife2017
Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Tunable AMPA receptor function via recurrent evolution of heterotetramers.The Journal of general physiology · 2026Article
- Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.Science (New York, N.Y.) · 2026Article
- Article
- Article
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
- Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.Nature structural & molecular biology · 2024Article
- Tuning synaptic strength by regulation of AMPA glutamate receptor localization.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- Female GluA3-KO mice show early onset hearing loss and afferent swellings in ambient sound levels.bioRxiv : the preprint server for biology · 2024Article
- Article
- Article
- Structure, Function, and Regulation of the Kainate Receptor.Sub-cellular biochemistry · 2022Review
- Structural and compositional diversity in the kainate receptor family.Cell reports · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021Review
- Article
- Subunit-selective iGluR antagonists can potentiate heteromeric receptor responses by blocking desensitization.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Quantitative Analysis of Protein Self-Association by Sedimentation Velocity.Current protocols in protein science · 2020Article
- Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture.Nature structural & molecular biology · 2020Article
- Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery.Scientific reports · 2019Article
- All tubulins are not alike: Heterodimer dissociation differs among different biological sources.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Ion conductivity and the gating characteristics of tetrameric glutamate receptor ion channels are determined by their subunit composition. Competitive homo- and hetero-dimerization of their amino-terminal domains (ATDs) is a key step controlling assembly. Here we measured systematically the thermodynamic stabilities of homodimers and heterodimers of kainate and AMPA receptors using fluorescence-detected sedimentation velocity analytical ultracentrifugation. Measured affinities span many orders of magnitude, and complexes show large differences in kinetic stabilities. The association of kainate receptor ATD dimers is generally weaker than the association of AMPA receptor ATD dimers, but both show a general pattern of increased heterodimer stability as compared to the homodimers of their constituents, matching well physiologically observed receptor combinations. The free energy maps of AMPA and kainate receptor ATD dimers provide a framework for the interpretation of observed receptor subtype combinations and possible assembly pathways.
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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.