ArticleBiochimica et biophysica acta. Biomembranes2020
The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.
Article in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Glutamate Ionotropic Kainate Receptors as Therapeutic Targets in Enzalutamide-Resistant and Neuroendocrine Prostate Cancer.International journal of molecular sciences · 2026Article
- JNJ-55511118 Stabilizes a Desensitized-like Conformation of γ8-Containing AMPA Receptors through Long-Range Allosteric Modulation.bioRxiv : the preprint server for biology · 2025Article
- Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor.Proteins · 2025Article
- Bi-directional allosteric pathway in NMDA receptor activation and modulation.Nature communications · 2024Article
- Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024Article
- 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
- Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.Membranes · 2021Article
- Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation.Nature communications · 2021Article
- Article
- Single molecule FRET methodology for investigating glutamate receptors.Methods in enzymology · 2021Article
- Allosteric Changes in the NMDA Receptor Associated with Calcium-Dependent Inactivation.Biophysical journal · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Kainate receptors, which are glutamate activated excitatory neurotransmitter receptors, predominantly exist as heteromers of GluK2 and GluK5 subunits in the mammalian central nervous system. There are currently no structures of the full-length heteromeric kainate receptors. Here, we have used single molecule FRET to determine the specific arrangement of the GluK2 and GluK5 subunits within the dimer of dimers configuration in a full-length receptor. Additionally, we have also studied the dynamics and conformational heterogeneity of the amino-terminal and agonist-binding domain interfaces associated with the resting and desensitized states of the full-length heteromeric kainate receptor using FRET-based methods. The smFRET data are compared to similar experiments performed on the homomeric kainate receptor to provide insight into the differences in conformational dynamics that distinguish the two functionally. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.
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