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

作者：Balasuriya Dilshan; Takahashi Hirohide; Srivats Shyam; Edwardson J Michael^*

来源：Biochemical and Biophysical Research Communications, 2014, 450(4): 1452-1457.

DOI：10.1016/j.bbrc.2014.07.009

• Ionotropic glutamate receptor
• NMDA receptor
• Excitatory glycine receptor
• Receptor activation
• Atomic force microscopy

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 similar to 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.

• 出版日期2014-8-8