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Title: Activation-induced structural change in the GluN1/GluN3A excitatory glycine receptor

Highlights: • We studied the response of the GluN1/GluN3A excitatory glycine receptor to activation. • GluN1 and GluN3A subunits interacted within transfected cells. • The GluN1/GluN3A receptor was functionally active. • Glycine or D-serine caused a ∼1 nm height reduction in bilayer-integrated receptors. • This height reduction was abolished by the glycine antagonist DCKA. - Abstract: Unlike GluN2-containing N-methyl-D-aspartate (NMDA) receptors, which require both glycine and glutamate for activation, receptors composed of GluN1 and GluN3 subunits are activated by glycine alone. Here, we used atomic force microscopy (AFM) imaging to examine the response to activation of the GluN1/GluN3A excitatory glycine receptor. GluN1 and GluN3A subunits were shown to interact intimately within transfected tsA 201 cells. Isolated GluN1/GluN3A receptors integrated into lipid bilayers responded to addition of either glycine or D-serine, but not glutamate, with a ∼1 nm reduction in height of the extracellular domain. The height reduction in response to glycine was abolished by the glycine antagonist 5,7-dichlorokynurenic acid. Our results represent the first demonstration of the effect of activation on the conformation of this receptor.
Authors:
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Publication Date:
OSTI Identifier:
22416692
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 450; Journal Issue: 4; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANIMAL CELLS; ATOMIC FORCE MICROSCOPY; ELECTROPHORESIS; GELS; GLYCINE; HUMAN POPULATIONS; KIDNEYS; LAYERS; LECITHINS; RECEPTORS; REDUCTION; SERINE