Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties

Weinan Sun, Kasper B. Hansen, Craig E. Jahr

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


During development of the central nervous system, there is a shift in the subunit composition of NMDA receptors (NMDARs) resulting in a dramatic 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 of diheteromeric 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 GluN2B subunit while having the kinetic properties of GluN1/2A NMDARs and highlight the complexity in NMDAR signaling created by diversity in subunit composition.

Original languageEnglish (US)
Pages (from-to)58-64.e3
Issue number1
StatePublished - Apr 5 2017


  • GluN2 subunit
  • Triheteromeric NMDA receptors
  • allosteric interaction
  • amino-terminal domain
  • crosslinking
  • excitatory synaptic transmission
  • glutamate
  • open probability
  • receptor deactivation

ASJC Scopus subject areas

  • Neuroscience(all)


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