N-Glycosylation Regulates the Trafficking and Surface Mobility of GluN3A-Containing NMDA Receptors

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F18%3A00492120" target="_blank" >RIV/67985823:_____/18:00492120 - isvavai.cz</a>

Alternative codes found

RIV/68378041:_____/18:00492865 RIV/00216208:11110/18:10389940 RIV/00216208:11310/18:10389940 RIV/00064165:_____/18:10389940

Result on the web

<a href="http://dx.doi.org/10.3389/fnmol.2018.00188" target="_blank" >http://dx.doi.org/10.3389/fnmol.2018.00188</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fnmol.2018.00188" target="_blank" >10.3389/fnmol.2018.00188</a>

Result language

angličtina

Original language name

N-Glycosylation Regulates the Trafficking and Surface Mobility of GluN3A-Containing NMDA Receptors

Original language description

N-methyl-D-aspartate receptors (NMDARs) play critical roles in both excitatory neurotransmission and synaptic plasticity. NMDARs containing the nonconventional GluN3A subunit have different functional properties compared to receptors comprised of GluN1/GluN2 subunits. Previous studies showed that GluN1/GluN2 receptors are regulated by N-glycosylation, however, limited information is available regarding the role of N-glycosylation in GluN3A-containing NMDARs. Using a combination of microscopy, biochemistry, and electrophysiology in mammalian cell lines and rat hippocampal neurons, we found that two asparagine residues (N203 and N368) in the GluN1 subunit and three asparagine residues (N145, N264 and N275) in the GluN3A subunit are required for surface delivery of GluN3A-containing NMDARs. Furthermore, deglycosylation and lectin-based analysis revealed that GluN3A subunits contain extensively modified N-glycan structures, including hybrid/complex forms of N-glycans. We also found (either using a panel of inhibitors or by studying human fibroblasts derived from patients with a congenital disorder of glycosylation) that N-glycan remodeling is not required for the surface delivery of GluN3A-containing NMDARs. Finally, we found that the surface mobility of GluN3A-containing NMDARs in hippocampal neurons is increased following incubation with 1-deoxymannojirimycin (DMM, an inhibitor of the formation of the hybrid/complex forms of N-glycans) and decreased in the presence of specific lectins. These findings provide new insight regarding the mechanisms by which neurons can regulate NMDAR trafficking and function.

Czech name

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Czech description

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Type

J_imp - 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)

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Frontiers in Molecular Neuroscience

ISSN

1662-5099

e-ISSN

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Volume of the periodical

11

Issue of the periodical within the volume

Jun 4

Country of publishing house

CH - SWITZERLAND

Number of pages

16

Pages from-to

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UT code for WoS article

000434052800001

EID of the result in the Scopus database

2-s2.0-85049017418