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An inter-dimer allosteric switch controls NMDA receptor activity.

Jean-Baptiste Esmenjaud1, David Stroebel1, Kelvin Chan2

  • 1Institut de Biologie de l'Ecole Normale Supérieure (IBENS), Ecole Normale Supérieure, Université PSL, CNRS, INSERM, Paris, France.

The EMBO Journal
|November 7, 2018
PubMed
Summary
This summary is machine-generated.

A novel rolling motion in NMDA receptors (NMDARs) controls channel activity. This mechanism, involving the agonist-binding domain layer, dictates receptor function and allosteric modulation, revealing key insights into neurotransmission.

Keywords:
NMDAallosteryglutamateligand‐gated ion channelreceptor

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biophysics

Background:

  • NMDA receptors (NMDARs) are crucial for excitatory neurotransmission and synaptic plasticity.
  • NMDARs form large complexes with eight extracellular domains, but their cooperative function is unclear.

Purpose of the Study:

  • To elucidate the mechanism by which NMDAR domains cooperate to control receptor activity.
  • To identify key structural determinants of NMDAR activation and allosteric modulation.

Main Methods:

  • Single-molecule and macroscopic electrophysiological recordings
  • Cysteine biochemistry
  • In silico analysis

Main Results:

  • A rolling motion at the interface between dimers in the agonist-binding domain (ABD) layer was identified as critical for NMDAR activation.
  • This rotation acts as a gating switch, influenced by the N-terminal domain (NTD) layer.
  • Locked-rolled NMDARs exhibit enhanced activity and resistance to NTD-mediated modulation.

Conclusions:

  • NMDAR domain movement is concerted, enabling long-range signal transduction.
  • A rolling motion in the ABD layer is a key determinant of NMDAR channel activity and allosteric control.