RGD Reference Report - Apparent homomeric NR1 currents observed in Xenopus oocytes are caused by an endogenous NR2 subunit. - Rat Genome Database

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Apparent homomeric NR1 currents observed in Xenopus oocytes are caused by an endogenous NR2 subunit.

Authors: Schmidt, Carsten  Hollmann, Michael 
Citation: Schmidt C and Hollmann M, J Mol Biol. 2008 Feb 22;376(3):658-70. doi: 10.1016/j.jmb.2007.11.105. Epub 2007 Dec 8.
RGD ID: 13432252
Pubmed: PMID:18177891   (View Abstract at PubMed)
DOI: DOI:10.1016/j.jmb.2007.11.105   (Journal Full-text)

Functional N-methyl-d-aspartate receptors NMDARs are thought to be heteromeric receptor complexes consisting of NR1 and NR2 subunits. However, recombinant NR1 subunits expressed in Xenopus oocytes assemble functional ion channels even without exogenous NR2 subunits and with a different pharmacology, suggesting a homomeric subunit stoichiometry. To explain this phenomenon, we screened oocytes for Xenopus NR2 subunits and found all four subunit-encoding mRNAs (XenNR2A-XenNR2D) to be present endogenously, with those encoding the XenNR2B subunit being particularly abundant. We cloned the full-length XenNR2B cDNA and co-expressed it with NR1 in oocytes. A detailed electrophysiological characterization revealed that the pharmacology of NR1/XenNR2B was identical with that of the presumed homomeric NMDARs expressed from NR1 subunits. By contrast, heteromeric receptors containing the rat NR2B subunit showed significant pharmacological differences compared with NR1/XenNR2B receptors. These results demonstrate that recombinant NR1 subunits expressed in Xenopus oocytes interact with an endogenously expressed NR2B subunit and form hybrid heteromeric NMDARs. These findings confirm the current views that NMDARs are obligatory heteromeric complexes and that functional homomeric NMDARs do not exist.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Grin1RatNMDA selective glutamate receptor complex part_ofIDA PMID:18177891UniProt 
Grin1Ratplasma membrane located_inIDA PMID:18177891UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Grin1RatNMDA glutamate receptor activity enablesIDA PMID:18177891UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Grin1  (glutamate ionotropic receptor NMDA type subunit 1)


Additional Information