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- Title
Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.
- Authors
Gonzalez, Cuauhtemoc U.; Carrillo, Elisa; Berka, Vladimir; Jayaraman, Vasanthi
- Abstract
Kainate receptors are members of the ionotropic glutamate receptor family. They form cation-specific transmembrane channels upon binding glutamate that desensitize in the continued presence of agonists. Concanavalin A (Con-A), a lectin, stabilizes the active open-channel state of the kainate receptor and reduces the extent of desensitization. In this study, we used single-molecule fluorescence resonance energy transfer (smFRET) to investigate the conformational changes underlying kainate receptor modulation by Con-A. These studies showed that Con-A binding to GluK2 homomeric kainate receptors resulted in closer proximity of the subunits at the dimer–dimer interface at the amino-terminal domain as well as between the subunits at the dimer interface at the agonist-binding domain. Additionally, the modulation of receptor functions by monovalent ions, which bind to the dimer interface at the agonist-binding domain, was not observed in the presence of Con-A. Based on these results, we conclude that Con-A modulation of kainate receptor function is mediated by a shift in the conformation of the kainate receptor toward a tightly packed extracellular domain.
- Subjects
FLUORESCENCE resonance energy transfer; GLUTAMATE receptors; CONCANAVALIN A; G protein coupled receptors
- Publication
Membranes, 2021, Vol 11, Issue 8, p613
- ISSN
2077-0375
- Publication type
Article
- DOI
10.3390/membranes11080613