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The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER
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SYSNO ASEP 0551559 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER Author(s) Horák, Martin (UEM-P) RID, ORCID
Baráčková, Petra (UEM-P)
Langore, Emily (UEM-P)
Netolický, Jakub (UEM-P)
Rivas-Ramirez, Paula (UEM-P)
Řeháková, Kristýna (UEM-P)Article number 603715 Source Title Frontiers in Neuroscience
Roč. 15, mar. (2021)Number of pages 12 s. Language eng - English Country CH - Switzerland Keywords disulfide bridges ; glutamate receptor ; glycosylation ; excitatory synapse ; posttranslational modification Subject RIV FH - Neurology OECD category Neurosciences (including psychophysiology R&D Projects GA20-12420S GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support UEM-P - RVO:68378041 UT WOS 000634722500001 EID SCOPUS 85103384539 DOI 10.3389/fnins.2021.603715 Annotation N-methyl-D-aspartate receptors (NMDARs) belong to a family of ionotropic glutamate receptors that play essential roles in excitatory neurotransmission and synaptic plasticity in the mammalian central nervous system (CNS). Functional NMDARs consist of heterotetramers comprised of GluN1, GluN2A-D, and/or GluN3A-B subunits, each of which contains four membrane domains (M1 through M4), an intracellular C-terminal domain, a large extracellular N-terminal domain composed of the amino-terminal domain and the S1 segment of the ligand-binding domain (LBD), and an extracellular loop between M3 and M4, which contains the S2 segment of the LBD. Both the number and type of NMDARs expressed at the cell surface are regulated at several levels, including their translation and posttranslational maturation in the endoplasmic reticulum (ER), intracellular trafficking via the Golgi apparatus, lateral diffusion in the plasma membrane, and internalization and degradation. This review focuses on the roles played by the extracellular regions of GluN subunits in ER processing. Specifically, we discuss the presence of ER retention signals, the integrity of the LBD, and critical N-glycosylated sites and disulfide bridges within the NMDAR subunits, each of these steps must pass quality control in the ER in order to ensure that only correctly assembled NMDARs are released from the ER for subsequent processing and trafficking to the surface. Finally, we discuss the effect of pathogenic missense mutations within the extracellular domains of GluN subunits with respect to ER processing of NMDARs. Workplace Institute of Experimental Medicine Contact Lenka Koželská, lenka.kozelska@iem.cas.cz, Tel.: 241 062 218, 296 442 218 Year of Publishing 2022 Electronic address https://www.frontiersin.org/articles/10.3389/fnins.2021.603715/full
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