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. 2021 Feb 10;17:1744806921990944. doi: 10.1177/1744806921990944

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© The Author(s) 2021

Creative Commons Non Commercial CC BY-NC: This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage).

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Figure 2. — Post-translational modifications (phosphorylation) of KA receptors. A number of residues within KA receptor subunits were shown to be phosphorylated, including S846/S868/S880/S886 (PKC), S856/S868 (PKA), S859/S892/T976 (CaMKII). All of these phosphorylation is shown to directly impact the kainite-evoked currents, and is also illustrated to be related to the endocytosis of KA receptors, leading to recycling of KA receptors to the membrane or degradation. Moreover, phosphorylation uncouples KA receptors from postsynaptic density 95 (PSD-95), improving the overall lateral mobility of these receptors by freeing them from synaptic incorporation. LBD ligand binding domain, GLU glutamate, N N-terminal domain, C C-terminal domain, P phosphorylation, EC extracellular, IC intracellular.