Madry, Christian ; Mesic, Ivana ; Bartholomäus, Ingo ; Nicke, Annette ; Betz, Heinrich ; Laube, Bodo (2007)
Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function.
In: Biochemical and biophysical research communications, 354 (1)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Calcium-permeable N-methyl-d-aspartate (NMDA) receptors are tetrameric cation channels composed of glycine-binding NR1 and glutamate-binding NR2 subunits, which require binding of both glutamate and glycine for efficient channel gating. In contrast, receptors assembled from NR1 and NR3 subunits function as calcium-impermeable excitatory glycine receptors that respond to agonist application only with low efficacy. Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Our results establish differential roles of the high-affinity NR3 and low-affinity NR1 glycine-binding sites in excitatory glycine receptor function.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2007 |
| Autor(en): | Madry, Christian ; Mesic, Ivana ; Bartholomäus, Ingo ; Nicke, Annette ; Betz, Heinrich ; Laube, Bodo |
| Art des Eintrags: | Bibliographie |
| Titel: | Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function. |
| Sprache: | Englisch |
| Publikationsjahr: | 2007 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Biochemical and biophysical research communications |
| Jahrgang/Volume einer Zeitschrift: | 354 |
| (Heft-)Nummer: | 1 |
| Kurzbeschreibung (Abstract): | Calcium-permeable N-methyl-d-aspartate (NMDA) receptors are tetrameric cation channels composed of glycine-binding NR1 and glutamate-binding NR2 subunits, which require binding of both glutamate and glycine for efficient channel gating. In contrast, receptors assembled from NR1 and NR3 subunits function as calcium-impermeable excitatory glycine receptors that respond to agonist application only with low efficacy. Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Our results establish differential roles of the high-affinity NR3 and low-affinity NR1 glycine-binding sites in excitatory glycine receptor function. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme ?? fb10_zoologie ?? |
| Hinterlegungsdatum: | 11 Apr 2011 09:26 |
| Letzte Änderung: | 05 Mär 2019 06:48 |
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