ArticleNature communications2014
Radial symmetry in a chimeric glutamate receptor pore.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Mapping the multi-domain allosteric network for CKAMP44 modulation of AMPA receptors.The Journal of biological chemistry · 2026Article
- TwoeLife · 2021Article
- Distinct GluN1 and GluN2 Structural Determinants for Subunit-Selective Positive Allosteric Modulation ofACS chemical neuroscience · 2021Article
- Prying open a glutamate receptor gate.The Journal of general physiology · 2019Article
- Cadmium opens GluK2 kainate receptors with cysteine substitutions at the M3 helix bundle crossing.The Journal of general physiology · 2019Article
- Glutamate-activated BK channel complexes formed with NMDA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Two adjacent phenylalanines in the NMDA receptor GluN2A subunit M3 domain interactively regulate alcohol sensitivity and ion channel gating.Neuropharmacology · 2017Article
- Chimeric Glutamate Receptor Subunits Reveal the Transmembrane Domain Is Sufficient for NMDA Receptor Pore Properties but Some Positive Allosteric Modulators Require Additional Domains.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels.Nature structural & molecular biology · 2016Review
- Kainate receptor pore-forming and auxiliary subunits regulate channel block by a novel mechanism.The Journal of physiology · 2016Article
- Ionotropic glutamate receptors: alive and kicking.The Journal of physiology · 2015Article
- Glutamatergic Transmission: A Matter of Three.Neural plasticity · 2015Review
- Glutamate receptor pores.The Journal of physiology · 2015Review
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Authors and funding
3 authors.
Funding
Abstract
Ionotropic glutamate receptors comprise two conformationally different A/C and B/D subunit pairs. Closed channels exhibit fourfold radial symmetry in the transmembrane domain (TMD) but transition to twofold dimer-of-dimers symmetry for extracellular ligand binding and N-terminal domains. Here, to evaluate symmetry in open pores we analysed interaction between the Q/R editing site near the pore loop apex and the transmembrane M3 helix of kainate receptor subunit GluK2. Chimeric subunits that combined the GluK2 TMD with extracellular segments from NMDA receptors, which are obligate heteromers, yielded channels made up of A/C and B/D subunit pairs with distinct substitutions along M3 and/or Q/R site editing status, in an otherwise identical homotetrameric TMD. Our results indicate that Q/R site interaction with M3 occurs within individual subunits and is essentially the same for both A/C and B/D subunit conformations, suggesting that fourfold pore symmetry persists in the open state.
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