The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378041%3A_____%2F21%3A00551559" target="_blank" >RIV/68378041:_____/21:00551559 - isvavai.cz</a>
Result on the web
<a href="https://www.frontiersin.org/articles/10.3389/fnins.2021.603715/full" target="_blank" >https://www.frontiersin.org/articles/10.3389/fnins.2021.603715/full</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3389/fnins.2021.603715" target="_blank" >10.3389/fnins.2021.603715</a>
Alternative languages
Result language
angličtina
Original language name
The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30103 - Neurosciences (including psychophysiology)
Result continuities
Project
<a href="/en/project/GA20-12420S" target="_blank" >GA20-12420S: Delineating the mechanisms that regulate specific NMDA receptor subtypes in mammalian neurones</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Frontiers in Neuroscience
ISSN
1662-453X
e-ISSN
1662-453X
Volume of the periodical
15
Issue of the periodical within the volume
mar.
Country of publishing house
CH - SWITZERLAND
Number of pages
12
Pages from-to
603715
UT code for WoS article
000634722500001
EID of the result in the Scopus database
2-s2.0-85103384539