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Molecular determinants for the strictly compartmentalized expression of kainate receptors in CA3 pyramidal cells

Author

Listed:
  • Sabine Fièvre

    (Interdisciplinary Institute for Neuroscience, CNRS UMR 5297, University of Bordeaux)

  • Mario Carta

    (Interdisciplinary Institute for Neuroscience, CNRS UMR 5297, University of Bordeaux)

  • Ingrid Chamma

    (Interdisciplinary Institute for Neuroscience, CNRS UMR 5297, University of Bordeaux)

  • Virginie Labrousse

    (Interdisciplinary Institute for Neuroscience, CNRS UMR 5297, University of Bordeaux)

  • Olivier Thoumine

    (Interdisciplinary Institute for Neuroscience, CNRS UMR 5297, University of Bordeaux)

  • Christophe Mulle

    (Interdisciplinary Institute for Neuroscience, CNRS UMR 5297, University of Bordeaux)

Abstract

Distinct subtypes of ionotropic glutamate receptors can segregate to specific synaptic inputs in a given neuron. Using functional mapping by focal glutamate uncaging in CA3 pyramidal cells (PCs), we observe that kainate receptors (KARs) are strictly confined to the postsynaptic elements of mossy fibre (mf) synapses and excluded from other glutamatergic inputs and from extrasynaptic compartments. By molecular replacement in organotypic slices from GluK2 knockout mice, we show that the faithful rescue of KAR segregation at mf-CA3 synapses critically depends on the amount of GluK2a cDNA transfected and on a sequence in the GluK2a C-terminal domain responsible for interaction with N-cadherin. Targeted deletion of N-cadherin in CA3 PCs greatly reduces KAR content in thorny excrescences and KAR-EPSCs at mf-CA3 synapses. Hence, multiple mechanisms combine to confine KARs at mf-CA3 synapses, including a stringent control of the amount of GluK2 subunit in CA3 PCs and the recruitment/stabilization of KARs by N-cadherins.

Suggested Citation

  • Sabine Fièvre & Mario Carta & Ingrid Chamma & Virginie Labrousse & Olivier Thoumine & Christophe Mulle, 2016. "Molecular determinants for the strictly compartmentalized expression of kainate receptors in CA3 pyramidal cells," Nature Communications, Nature, vol. 7(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12738
    DOI: 10.1038/ncomms12738
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