The distal carboxyl terminal of rat NR3B subunit regulates NR1-1a/NR3B and NR1-2a/NR3B surface trafficking

Karen Siaw-Ling Wee; Zhen-Ning Wee; Nicholas Boon-How Chow; Chian-Ming Low

doi:10.1016/j.neuint.2010.05.003

The distal carboxyl terminal of rat NR3B subunit regulates NR1-1a/NR3B and NR1-2a/NR3B surface trafficking

Neurochem Int. 2010 Sep;57(2):97-101. doi: 10.1016/j.neuint.2010.05.003. Epub 2010 May 11.

Authors

Karen Siaw-Ling Wee¹, Zhen-Ning Wee, Nicholas Boon-How Chow, Chian-Ming Low

Affiliation

¹ Department of Pharmacology, Yong Loo Lin School of Medicine, National University of Singapore, Republic of Singapore.

PMID: 20466026
DOI: 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Immunohistochemistry
Mutagenesis, Site-Directed
Protein Transport
Rats
Receptors, N-Methyl-D-Aspartate / chemistry
Receptors, N-Methyl-D-Aspartate / genetics
Receptors, N-Methyl-D-Aspartate / metabolism*

Substances

Receptors, N-Methyl-D-Aspartate