Journal
NEURON
Volume 94, Issue 1, Pages 58-+Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2017.03.018
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Funding
- National Institutes of Health [R21NS091337, P20GM103546, R01NS097536]
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During development of the central nervous system, there is a shift in the subunit composition of NMDA receptors(NMDARs) resultingin adramatic acceleration of NMDAR-mediated synaptic currents. This shift coincides with upregulation of the GluN2A subunit and triheteromeric GluN1/2A/2B receptors with fast deactivation kinetics, whereas expression ofdiheteromeric GluN1/2B receptors with slower deactivation kinetics is decreased. Here, we show that allosteric interactions occur between the glutamate-binding GluN2 subunits in triheteromeric GluN1/2A/2B NMDARs. This allosterism is dominated by the GluN2A subunit and results in functional properties not predicted by those of diheteromeric GluN1/2A and GluN1/2B NMDARs. These findings suggest that GluN1/2A/2B NMDARs may maintain some signaling properties of the GluN2Bsubunit while having the kinetic properties of GluN1/2A NMDARs and highlight the complexity in NMDAR signaling created by diversity in subunit composition.
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