Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-D-aspartate (NMDA) Receptors from the Endoplasmic Reticulum

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10316307" target="_blank" >RIV/00216208:11310/15:10316307 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/15:00447505
Result on the web
<a href="http://dx.doi.org/10.1074/jbc.M115.656546" target="_blank" >http://dx.doi.org/10.1074/jbc.M115.656546</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M115.656546" target="_blank" >10.1074/jbc.M115.656546</a>

Result language
angličtina
Original language name
Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-D-aspartate (NMDA) Receptors from the Endoplasmic Reticulum
Original language description
NMDA receptors (NMDARs) comprise a subclass of neurotransmitter receptors whose surface expression is regulated at multiple levels, including processing in the endoplasmic reticulum (ER), intracellular trafficking via the Golgi apparatus, internalization, recycling, anddegradation. With respect to early processing, NMDARs are regulated by the availability of GluN subunits within the ER, the presence of ER retention and export signals, and post translational modifications, including phosphorylation and palmitoylation. However, the role of N-glycosylation, one of the most common posttranslational modifications, in regulating NMDAR processing has not been studied in detail. Using biochemistry, confocal and electron microscopy, and electrophysiology in conjunction with a lentivirus-based molecular replacement strategy, we found that NMDARs are released from the ER only when two asparagine residues in the GluN1 subunit (Asn-203 and Asn-368) are N-glycosylated. Although the GluN2A and GluN2B
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FH - Neurology, neuro-surgery, nuero-sciences
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
S - Specificky vyzkum na vysokych skolach

Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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