Cousins, S.L., Kenny, A.V. and Stephenson, F.A. (2009) Delineation of additional PSD-95 binding domains within NMDA receptor NR2 subunits reveals differences between NR2A/PSD-95 and NR2B/PSD-95 association. Neuroscience, 158 (1). pp. 89-95. 10.1016/j.neuroscience.2007.12.051.
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N-methyl-d-aspartate (NMDA) receptors are clustered at synapses via their association with the PSD-95 (post-synaptic density-95) membrane associated guanylate kinase (MAGUK) family of scaffolding proteins. PSD-95 is the best characterized of this family. It is known to associate with NMDA receptor NR2 subunits via a conserved ES(E/D)V amino acid sequence located at their C-termini and thus to promote the clustering, regulation and the trafficking of assembled NR1/NR2 NMDA receptors at synapses. Here we have investigated in more detail NMDA receptor NR2/PSD-95 protein–protein association. Wild-type NR1 and PSD-95α were co-expressed with a series of rodent C-terminal truncated constructs of either NR2A or NR2B subunits in human embryonic kidney (HEK) 293 cells and the association of PSD-95α with assembled receptors determined by immunoprecipitation. Additional PSD-95 binding domains that differed between NR2A and NR2B subunits were identified. These domains mapped to the amino acid sequences NR2A (1382–1420) and NR2B (1086–1157). These results suggest that NR2A and NR2B may associate with PSD-95 but with different affinities. This may be important in the determination of the lateral mobility of NMDA receptor subtypes in post-synaptic membranes.
|Additional Information:||Full text available electronically from the School of Pharmacy Library.|
|Uncontrolled Keywords:||glutamate receptor; glutamate; scaffolding proteins; receptor trafficking|
|Departments, units and centres:||Department of Pharmacology > Department of Pharmacology|
|Journal or Publication Title:||Neuroscience|
|Deposited By:||Library Staff|
|Deposited On:||28 Apr 2009 09:35|
|Last Modified:||24 Nov 2011 14:40|
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