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Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-D-aspartate (NMDA) Receptors from the Endoplasmic Reticulum
- 1.0447505 - FGÚ 2016 RIV US eng J - Journal Article
Lichnerová, Katarina - Kaniaková, Martina - Park, S. P. - Skřenková, Kristýna - Wang, Y.- X. - Petralia, R. S. - Suh, Y. H. - Horák, Martin
Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-D-aspartate (NMDA) Receptors from the Endoplasmic Reticulum.
Journal of Biological Chemistry. Roč. 290, č. 30 (2015), s. 18379-18390. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR(CZ) GA14-02219S; GA MŠMT(CZ) ED1.1.00/02.0109
Institutional support: RVO:67985823
Keywords : peptide-N-glycosidase * NMDAR * NMDA receptor * endoplasmic reticulum
Subject RIV: FH - Neurology
Impact factor: 4.258, year: 2015
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
Permanent Link: http://hdl.handle.net/11104/0249342
Number of the records: 1