Link to bioRxiv paper:

http://biorxiv.org/cgi/content/short/2020.08.21.261388v1?rss=1

Authors: Amico-Ruvio, S. A., Paganelli, M. A., Abbott, J. A., Myers, J. M., Kasperek, E. M., Iacobucci, G. J., Popescu, G. K.

Abstract:

To investigate the role of the N-terminal do-mains (NTDs) in NMDA receptor signaling we used kinetic analyses of one-channel currents and compared the reaction mechanism of re-combinant wild-type GluN1/GluN2A and GluN1/GluN2B receptors with those observed for NDT-lacking receptors. We found that trun-cated receptors maintained the fundamental gat-ing mechanism characteristic of NMDA recep-tors, which includes a multi-state activation se-quence, desensitization steps, and mode transi-tions. This result establishes that none of the functionally-defined NMDA receptor activation events require the NTD. Notably, receptors that lacked the entire NTD layer retained isoform-specific kinetics. Together with previous reports, these results demonstrate that the entire gating machinery of NMDA receptors resides within a core domain that contains the ligand-binding and the channel-forming transmembrane domains, whereas the NTD and C-terminal layers serve modulatory functions, exclusively

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