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hal.structure.identifierCenter for Neuroscience and Cell Biology (CNC) [CNC]
dc.contributor.authorKELLERMAYER, Blanka
dc.contributor.authorFERREIRA, Joana
dc.contributor.authorDUPUIS, Julien
dc.contributor.authorLEVET, Florian
dc.contributor.authorGRILLO-BOSCH, Dolors
dc.contributor.authorBARD, Lucie
dc.contributor.authorLINARÈS-LOYEZ, Jeanne
dc.contributor.authorBOUCHET, Delphine
dc.contributor.authorCHOQUET, Daniel
dc.contributor.authorRUSAKOV, Dmitri
dc.contributor.authorBON, Pierre
dc.contributor.authorSIBARITA, Jean-Baptiste
hal.structure.identifierLaboratoire Photonique, Numérique et Nanosciences [LP2N]
hal.structure.identifierLP2N_G8, LP2N_A3
dc.contributor.authorCOGNET, Laurent
dc.contributor.authorSAINLOS, Matthieu
hal.structure.identifierUnidade de Ciencias Biomoleculares Aplicadas [UCIBIO]
dc.contributor.authorCARVALHO, Ana Luisa
dc.contributor.authorGROC, Laurent
dc.date.accessioned2023-05-12T10:48:48Z
dc.date.available2023-05-12T10:48:48Z
dc.date.issued2018-10
dc.identifier.issn0896-6273
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/181784
dc.description.abstractEnNMDA 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.isoen
dc.publisherElsevier
dc.subject.endSTORM
dc.subject.enGluN2
dc.subject.enSingle molecule
dc.subject.enGlutamate receptor
dc.subject.enSubunit synapse
dc.title.enDifferential Nanoscale Topography and Functional Role of GluN2-NMDA Receptor Subtypes at Glutamatergic Synapses
dc.typeArticle de revue
dc.identifier.doi10.1016/j.neuron.2018.09.012
dc.subject.halPhysique [physics]/Physique [physics]/Biophysique [physics.bio-ph]
bordeaux.journalNeuron
bordeaux.page106 - 119.e7
bordeaux.volume100
bordeaux.hal.laboratoriesLaboratoire Photonique, Numérique et Nanosciences (LP2N) - UMR 5298*
bordeaux.issue1
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
hal.identifierhal-01914542
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01914542v1
bordeaux.COinSctx_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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