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Article
Nature Neuroscience  6, 476 - 483 (2003)
Published online: 7 April 2003; | doi:10.1038/nn1044

Modal gating of NMDA receptors and the shape of their synaptic response

Gabriela Popescu & Anthony Auerbach

Center for Single Molecule Biophysics and the Department of Physiology and Biophysics, School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York 14214, USA

Correspondence should be addressed to Gabriela Popescu popescu@buffalo.edu or Anthony Auerbach auerbach@buffalo.edu
N-methyl-D-aspartate receptor (NMDAR) channels mediate the slow component of excitatory potentials at glutamatergic synapses. They have complex kinetic behavior, and much remains to be understood about NMDAR gating mechanisms and the molecular events that shape the synaptic current. Here we show that an individual NMDAR produces at least three stable patterns of activity. For all modes, channels gate by the same mechanism and can occupy either of two open states. The relative stability of the open states differs across modes because of a common perturbation to the NMDAR structure that may be subject to cellular control. Simulations indicate that native NMDAR-mediated synaptic responses arise mainly from the most common mode, and that the slow rise and decay of the current can be attributed to multiple transitions between fully liganded open and closed states rather than to agonist dissociation.

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REFERENCE
NMDA Receptors
Nature Encyclopaedia of Life Sciences

REVIEWS
Src kinases: a hub for NMDA receptor regulation
Nature Reviews Neuroscience Review (01 Apr 2004)

RESEARCH
Regulation of ATP-sensitive potassium channel function by protein kinase A-mediated phosphorylation in transfected HEK293 cells
The EMBO Journal Article (01 Mar 2000)
Excitatory glycine receptors containing the NR3 family of NMDA receptor subunits
Nature Letters to Editor (14 Feb 2002)
Cooperation between independent hippocampal synapses is controlled by glutamate uptake
Nature Neuroscience Article (01 Apr 2002)
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Nature Neuroscience
ISSN: 1097-6256
EISSN: 1546-1726
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