@article {1159, title = {Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery [National Cryo-Electron Microscopy Facility]}, journal = {Sci Rep}, volume = {9}, year = {2019}, month = {2019 Jul 16}, pages = {10254}, abstract = {
GluK3-kainate receptors are atypical members of the iGluR family that reside at both the pre- and postsynapse and play a vital role in the regulation of synaptic transmission. For a better understanding of structural changes that underlie receptor functions, GluK3 receptors were trapped in desensitized and resting/closed states and structures analyzed using single particle cryo-electron microscopy. While the desensitized GluK3 has domain organization as seen earlier for another kainate receptor-GluK2, antagonist bound GluK3 trapped a resting state with only two LBD domains in dimeric arrangement necessary for receptor activation. Using structures as a guide, we show that the N-linked glycans at the interface of GluK3 ATD and LBD likely mediate inter-domain interactions and attune receptor-gating properties. The mutational analysis also identified putative N-glycan interacting residues. Our results provide a molecular framework for understanding gating properties unique to GluK3 and exploring the role of N-linked glycosylation in their modulation.
}, issn = {2045-2322}, doi = {10.1038/s41598-019-46770-z}, author = {Kumari, Jyoti and Vinnakota, Rajesh and Kumar, Janesh} }