Journal
NEURON
Volume 100, Issue 1, Pages 106-+Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2018.09.012
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Funding
- Erasmus Mundus Joint Doctorate (EMJD) program (European Neuroscience Campus)
- Programme d'Actions Universitaires Integres Luso-Francaises (2016/2017)
- Programme d'Actions Universitaires Integres Luso-Francaises (2017/2018)
- Agence Nationale de la Recherche [ANR-14-OHRI-0001-01, ANR-15-CE16-0004-03]
- Centre National de la Recherche Scientifique
- IdEx Bordeaux [ANR-10-IDEX-03-02]
- Fondation pour la Recherche Medicale
- Human Frontier Science Program [RGP0019]
- postdoctoral Marie-Curie Intra-European fellowship [neuroCHEMbiotools 273817]
- Conseil Regional d'Aquitaine
- Wellcome Trust [101896/Z/13/Z]
- ERC advanced grant ADOS
- Labex Bordeaux BRAIN
- Agence Nationale de la Recherche (ANR) [ANR-14-OHRI-0001, ANR-15-CE16-0004] Funding Source: Agence Nationale de la Recherche (ANR)
- Wellcome Trust [101896/Z/13/Z] Funding Source: Wellcome Trust
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NMDA receptors (NMDARs) play key roles in the use-dependent adaptation of glutamatergic synapses underpinning memory formation. In the forebrain, these plastic processes involve the varied contributions of GluN2A- and GluN2B-containing NMDARs that have different signaling properties. Although the molecular machinery of synaptic NMDAR trafficking has been under scrutiny, the postsynaptic spatial organization of these two receptor subtypes has remained elusive. Here, we used super-resolution imaging of NMDARs in rat hippocampal synapses to unveil the nanoscale topography of native GluN2A- and GluN2B-NMDARs. Both subtypes were found to be organized in separate nanodomains that vary over the course of development. Furthermore, GluN2A-and GluN2B-NMDAR nanoscale organizations relied on distinct regulatory mechanisms. Strikingly, the selective rearrangement of GluN2A-and GluN2B-NMDARs, with no overall change in NMDAR current amplitude, allowed bi-directional tuning of synaptic LTP. Thus, GluN2A-and GluN2B-NMDAR nanoscale organizations are differentially regulated and seem to involve distinct signaling complexes during synaptic adaptation.
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