TY  - INPR
N1  - This version is the author accepted manuscript. For information on re-use, please refer to the publisher?s terms and conditions.
TI  - Differential Nanoscale Topography and Functional Role of GluN2-NMDA Receptor Subtypes at Glutamatergic Synapses
EP  - 14
Y1  - 2018/10/10/
AV  - public
VL  - 100
SP  - 1
JF  - Neuron
KW  - glutamate receptor
KW  -  dSTORM
KW  -  single molecule
KW  -  GluN2 subunit
KW  -  synapse
A1  - Kellermayer, B
A1  - Ferreira, JS
A1  - Dupuis, J
A1  - Levet, F
A1  - Grillo-Bosch, D
A1  - Bard, L
A1  - Linarès-Loyez, J
A1  - Bouchet, D
A1  - Choquet, D
A1  - Rusakov, DA
A1  - Bon, P
A1  - Sibarita, J-B
A1  - Cognet, L
A1  - Sainlos, M
A1  - Carvalho, AL
A1  - Groc, L
ID  - discovery10057901
N2  - 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.
SN  - 0896-6273
UR  - https://doi.org/10.1016/j.neuron.2018.09.012
ER  -