Signal peptide represses GluK1 surface and synaptic trafficking through binding to amino-terminal domain

Gui-Fang Duan, Yaxin Ye, Sha Xu, Wucheng Tao, Shiping Zhao, Tengchuan Jin, Roger A. Nicoll, Yun Stone Shi () and Nengyin Sheng ()
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Gui-Fang Duan: Nanjing University
Yaxin Ye: Kunming Institute of Zoology, Chinese Academy of Sciences
Sha Xu: Kunming Institute of Zoology, Chinese Academy of Sciences
Wucheng Tao: University of California
Shiping Zhao: Kunming Institute of Zoology, Chinese Academy of Sciences
Tengchuan Jin: School of Life Sciences and Medical Center, University of Science and Technology of China
Roger A. Nicoll: University of California
Yun Stone Shi: Nanjing University
Nengyin Sheng: Kunming Institute of Zoology, Chinese Academy of Sciences

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract Kainate-type glutamate receptors play critical roles in excitatory synaptic transmission and synaptic plasticity in the brain. GluK1 and GluK2 possess fundamentally different capabilities in surface trafficking as well as synaptic targeting in hippocampal CA1 neurons. Here we find that the excitatory postsynaptic currents (EPSCs) are significantly increased by the chimeric GluK1(SPGluK2) receptor, in which the signal peptide of GluK1 is replaced with that of GluK2. Coexpression of GluK1 signal peptide completely suppresses the gain in trafficking ability of GluK1(SPGluK2), indicating that the signal peptide represses receptor trafficking in a trans manner. Furthermore, we demonstrate that the signal peptide directly interacts with the amino-terminal domain (ATD) to inhibit the synaptic and surface expression of GluK1. Thus, we have uncovered a 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 forward trafficking of the receptor.

Date: 2018
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DOI: 10.1038/s41467-018-07403-7

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