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Article

Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions

1
Department of Biological Chemistry, Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan
2
Department of Integrative Physiology, Faculty of Medicine, University of Miyazaki, Miyazaki 889-1692, Japan
3
Department of Molecular Cell Biology, Faculty of Medical Technology, Graduate School of Health Sciences, Fujita Health University, Aichi 470-1192, Japan
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2020, 21(14), 5101; https://doi.org/10.3390/ijms21145101
Received: 15 June 2020 / Revised: 14 July 2020 / Accepted: 17 July 2020 / Published: 19 July 2020
(This article belongs to the Special Issue Function and Expression of Neural Glycans)
The AMPA-type glutamate receptor (AMPAR) is a homotetrameric or heterotetrameric ion channel composed of various combinations of four subunits (GluA1–4), and its abundance in the synapse determines the strength of synaptic activity. The formation of oligomers in the endoplasmatic reticulum (ER) is crucial for AMPAR subunits’ ER-exit and translocation to the cell membrane. Although N-glycosylation on different AMPAR subunits has been shown to regulate the ER-exit of hetero-oligomers, its role in the ER-exit of homo-oligomers remains unclear. In this study, we investigated the role of N-glycans at GluA1N63/N363 and GluA2N370 in ER-exit under the homo-oligomeric expression conditions, whose mutants are known to show low cell surface expressions. In contrast to the N-glycosylation site mutant GluA1N63Q, the cell surface expression levels of GluA1N363Q and GluA2N370Q increased in a time-dependent manner. Unlike wild-type (WT) GluA1, GluA2WT rescued surface GluA2N370Q expression. Additionally, the expression of GluA1N63Q reduced the cell surface expression level of GluA1WT. In conclusion, our findings suggest that these N-glycans have distinct roles in the ER-exit of GluA1 and GluA2 homo-oligomers; N-glycan at GluA1N63 is a prerequisite for GluA1 ER-exit, whereas N-glycans at GluA1N363 and GluA2N370 control the ER-exit rate. View Full-Text
Keywords: AMPA-type glutamate receptor; GluA1; GluA2; N-glycan AMPA-type glutamate receptor; GluA1; GluA2; N-glycan
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MDPI and ACS Style

Morise, J.; Yamamoto, S.; Midorikawa, R.; Takamiya, K.; Nonaka, M.; Takematsu, H.; Oka, S. Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions. Int. J. Mol. Sci. 2020, 21, 5101. https://doi.org/10.3390/ijms21145101

AMA Style

Morise J, Yamamoto S, Midorikawa R, Takamiya K, Nonaka M, Takematsu H, Oka S. Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions. International Journal of Molecular Sciences. 2020; 21(14):5101. https://doi.org/10.3390/ijms21145101

Chicago/Turabian Style

Morise, Jyoji, Saki Yamamoto, Ryosuke Midorikawa, Kogo Takamiya, Motohiro Nonaka, Hiromu Takematsu, and Shogo Oka. 2020. "Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions" International Journal of Molecular Sciences 21, no. 14: 5101. https://doi.org/10.3390/ijms21145101

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