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Identity of endogenous NMDAR glycine site agonist in amygdala is determined by synaptic activity level

Author

Listed:
  • Yan Li

    (McLean Hospital, Harvard Medical School)

  • Silvia Sacchi

    (University of Insubria, ‘The Protein Factory’ Research Center for Protein Biotechnologies, Politecnico di Milano and University of Insubria)

  • Loredano Pollegioni

    (University of Insubria, ‘The Protein Factory’ Research Center for Protein Biotechnologies, Politecnico di Milano and University of Insubria)

  • Alo C. Basu

    (McLean Hospital, Harvard Medical School)

  • Joseph T. Coyle

    (McLean Hospital, Harvard Medical School)

  • Vadim Y. Bolshakov

    (McLean Hospital, Harvard Medical School)

Abstract

Mechanisms of N-methyl-D-aspartate receptor-dependent synaptic plasticity contribute to the acquisition and retention of conditioned fear memory. However, synaptic rules which may determine the extent of N-methyl-D-aspartate receptor activation in the amygdala, a key structure implicated in fear learning, remain unknown. Here we show that the identity of the N-methyl-D-aspartate receptor glycine site agonist at synapses in the lateral nucleus of the amygdala may depend on the level of synaptic activation. Tonic activation of N-methyl-D-aspartate receptors at synapses in the amygdala under low activity conditions is supported by ambient D-serine, whereas glycine may be released from astrocytes in response to afferent impulses. The release of glycine may decode the increases in afferent activity levels into enhanced N-methyl-D-aspartate receptor-mediated synaptic events, serving an essential function in the induction of N-methyl-D-aspartate receptor-dependent long-term potentiation in fear conditioning pathways.

Suggested Citation

  • Yan Li & Silvia Sacchi & Loredano Pollegioni & Alo C. Basu & Joseph T. Coyle & Vadim Y. Bolshakov, 2013. "Identity of endogenous NMDAR glycine site agonist in amygdala is determined by synaptic activity level," Nature Communications, Nature, vol. 4(1), pages 1-11, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2779
    DOI: 10.1038/ncomms2779
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