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- W2914519694 abstract "Kainate-type glutamate receptors play critical roles in excitatory synaptic transmission and synaptic plasticity. GluK1 and GluK2 are two major subunits of kainate receptors expressed in brain. Previously we have found that they possess fundamentally different capabilities in surface trafficking as well as synaptic targeting in hippocampal CA1 neurons. To pinpoint the underlying molecular mechanism, we construct chimeric receptors by swapping different domains between GluK1 and GluK2. Intriguingly, we find that the EPSCs are increased significantly by the chimera GluK1(SPGluK2), in which the GluK1 signal peptide is replaced with that of GluK2. Coexpression of GluK1 signal peptide completely suppresses the gained trafficking ability of GluK1(SPGluK2), indicating the signal peptide represses the receptor trafficking in a trans manner. Furthermore, we demonstrate that the signal peptide interplays with the amino-terminal domain (ATD) to inhibit GluK1 receptor synaptic and surface expression and these two functional domains interact directly. Thus, we have uncovered a novel trafficking mechanism for kainate receptors and propose that the cleaved signal peptide behaves as a ligand of GluK1, through binding with the ATD, to repress GluK1 forward trafficking." @default.
- W2914519694 created "2019-02-21" @default.
- W2914519694 creator A5022721940 @default.
- W2914519694 date "2019-02-01" @default.
- W2914519694 modified "2023-09-30" @default.
- W2914519694 title "Signal Peptide Represses Kainate Receptor GluK1 Surface and Synaptic Trafficking through Direct Interaction with Amino-Terminal Domain" @default.
- W2914519694 doi "https://doi.org/10.1016/j.bpj.2018.11.613" @default.
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