Please use this identifier to cite or link to this item:
|Title:||The distal carboxyl terminal of rat NR3B subunit regulates NR1-1a/NR3B and NR1-2a/NR3B surface trafficking|
|Authors:||Wee, K.S.L. |
|Source:||Wee, K.S.L., Wee, Z.-N., Chow, N.B.H., Low, C.-M. (2010). The distal carboxyl terminal of rat NR3B subunit regulates NR1-1a/NR3B and NR1-2a/NR3B surface trafficking. Neurochemistry International 57 (2) : 97-101. ScholarBank@NUS Repository. https://doi.org/10.1016/j.neuint.2010.05.003|
|Abstract:||N-Methyl-. d-aspartate (NMDA) receptors are multi-subunit receptors formed from assembly of NR1 with NR2 and/or NR3 subunits. In this study, we investigated the role of a conserved RERLR motif present in a region within the distal carboxyl terminal of rat NR3B (between residues 952 and 984) in targeting NR1-1a/NR3B and NR1-2a/NR3B receptors to the cell surface. Surface biotinylation, confocal immunofluorescence microscopy and site-directed mutagenesis studies showed RERLR motif does not influence the surface expression of NR1-1a/NR3B NMDA receptor complex. Our bioinformatics analysis further showed this region can also exist as a coiled-coil domain. Truncation of this putative coiled-coil domain in NR3B affects surface expression of NR1-1a/NR3B and NR1-2a/NR3B receptors similarly suggesting that NR1 C1 cassette is not involved in the effect mediated by the distal carboxyl region of NR3B. This study represents the first attempt to evaluate a specific motif in regulating rat NR3B surface expression. © 2010 Elsevier Ltd.|
|Source Title:||Neurochemistry International|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 14, 2018
WEB OF SCIENCETM
checked on Jan 23, 2018
checked on Feb 19, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.