Madry, Christian, et al. "Principal Role of NR3 Subunits in NR1/NR3 Excitatory Glycine Receptor Function." Biochemical and Biophysical Research Communications, vol. 354, no. 1, 2007, pp. 102-8.
Madry C, Mesic I, Bartholomäus I, et al. Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function. Biochem Biophys Res Commun. 2007;354(1):102-8.
Madry, C., Mesic, I., Bartholomäus, I., Nicke, A., Betz, H., & Laube, B. (2007). Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function. Biochemical and Biophysical Research Communications, 354(1), 102-8.
Madry C, et al. Principal Role of NR3 Subunits in NR1/NR3 Excitatory Glycine Receptor Function. Biochem Biophys Res Commun. 2007 Mar 2;354(1):102-8. PubMed PMID: 17214961.
TY - JOUR
T1 - Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function.
AU - Madry,Christian,
AU - Mesic,Ivana,
AU - Bartholomäus,Ingo,
AU - Nicke,Annette,
AU - Betz,Heinrich,
AU - Laube,Bodo,
Y1 - 2006/12/28/
PY - 2006/12/15/received
PY - 2006/12/19/accepted
PY - 2007/1/12/pubmed
PY - 2007/4/7/medline
PY - 2007/1/12/entrez
SP - 102
EP - 8
JF - Biochemical and biophysical research communications
JO - Biochem Biophys Res Commun
VL - 354
IS - 1
N2 - 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.
SN - 0006-291X
UR - https://www.unboundmedicine.com/medline/citation/17214961/Principal_role_of_NR3_subunits_in_NR1/NR3_excitatory_glycine_receptor_function_
L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(06)02825-7
DB - PRIME
DP - Unbound Medicine