Differential Nanoscale Topography and Functional Role of GluN2-NMDA Receptor Subtypes at Glutamatergic Synapses
hal.structure.identifier | Center for Neuroscience and Cell Biology (CNC) [CNC] | |
dc.contributor.author | KELLERMAYER, Blanka | |
dc.contributor.author | FERREIRA, Joana | |
dc.contributor.author | DUPUIS, Julien | |
dc.contributor.author | LEVET, Florian | |
dc.contributor.author | GRILLO-BOSCH, Dolors | |
dc.contributor.author | BARD, Lucie | |
dc.contributor.author | LINARÈS-LOYEZ, Jeanne | |
dc.contributor.author | BOUCHET, Delphine | |
dc.contributor.author | CHOQUET, Daniel | |
dc.contributor.author | RUSAKOV, Dmitri | |
dc.contributor.author | BON, Pierre | |
dc.contributor.author | SIBARITA, Jean-Baptiste | |
hal.structure.identifier | Laboratoire Photonique, Numérique et Nanosciences [LP2N] | |
hal.structure.identifier | LP2N_G8, LP2N_A3 | |
dc.contributor.author | COGNET, Laurent | |
dc.contributor.author | SAINLOS, Matthieu | |
hal.structure.identifier | Unidade de Ciencias Biomoleculares Aplicadas [UCIBIO] | |
dc.contributor.author | CARVALHO, Ana Luisa | |
dc.contributor.author | GROC, Laurent | |
dc.date.accessioned | 2023-05-12T10:48:48Z | |
dc.date.available | 2023-05-12T10:48:48Z | |
dc.date.issued | 2018-10 | |
dc.identifier.issn | 0896-6273 | |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/181784 | |
dc.description.abstractEn | 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. | |
dc.language.iso | en | |
dc.publisher | Elsevier | |
dc.subject.en | dSTORM | |
dc.subject.en | GluN2 | |
dc.subject.en | Single molecule | |
dc.subject.en | Glutamate receptor | |
dc.subject.en | Subunit synapse | |
dc.title.en | Differential Nanoscale Topography and Functional Role of GluN2-NMDA Receptor Subtypes at Glutamatergic Synapses | |
dc.type | Article de revue | |
dc.identifier.doi | 10.1016/j.neuron.2018.09.012 | |
dc.subject.hal | Physique [physics]/Physique [physics]/Biophysique [physics.bio-ph] | |
bordeaux.journal | Neuron | |
bordeaux.page | 106 - 119.e7 | |
bordeaux.volume | 100 | |
bordeaux.hal.laboratories | Laboratoire Photonique, Numérique et Nanosciences (LP2N) - UMR 5298 | * |
bordeaux.issue | 1 | |
bordeaux.institution | Université de Bordeaux | |
bordeaux.institution | CNRS | |
bordeaux.peerReviewed | oui | |
hal.identifier | hal-01914542 | |
hal.version | 1 | |
hal.origin.link | https://hal.archives-ouvertes.fr//hal-01914542v1 | |
bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Neuron&rft.date=2018-10&rft.volume=100&rft.issue=1&rft.spage=106%20-%20119.e7&rft.epage=106%20-%20119.e7&rft.eissn=0896-6273&rft.issn=0896-6273&rft.au=KELLERMAYER,%20Blanka&FERREIRA,%20Joana&DUPUIS,%20Julien&LEVET,%20Florian&GRILLO-BOSCH,%20Dolors&rft.genre=article |
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