RGD Reference Report - The cell adhesion molecule neuroplastin-65 is a novel interaction partner of gamma-aminobutyric acid type A receptors. - Rat Genome Database

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The cell adhesion molecule neuroplastin-65 is a novel interaction partner of gamma-aminobutyric acid type A receptors.

Authors: Sarto-Jackson, I  Milenkovic, I  Smalla, KH  Gundelfinger, ED  Kaehne, T  Herrera-Molina, R  Thomas, S  Kiebler, MA  Sieghart, W 
Citation: Sarto-Jackson I, etal., J Biol Chem. 2012 Apr 20;287(17):14201-14. doi: 10.1074/jbc.M111.293175. Epub 2012 Mar 2.
RGD ID: 9835374
Pubmed: PMID:22389504   (View Abstract at PubMed)
PMCID: PMC3340160   (View Article at PubMed Central)
DOI: DOI:10.1074/jbc.M111.293175   (Journal Full-text)

gamma-Aminobutyric acid type A (GABA(A)) receptors are pentameric ligand-gated ion channels that mediate fast inhibition in the central nervous system. Depending on their subunit composition, these receptors exhibit distinct pharmacological properties and differ in their ability to interact with proteins involved in receptor anchoring at synaptic or extra-synaptic sites. Whereas GABA(A) receptors containing alpha1, alpha2, or alpha3 subunits are mainly located synaptically where they interact with the submembranous scaffolding protein gephyrin, receptors containing alpha5 subunits are predominantly found extra-synaptically and seem to interact with radixin for anchorage. Neuroplastin is a cell adhesion molecule of the immunoglobulin superfamily that is involved in hippocampal synaptic plasticity. Our results reveal that neuroplastin and GABA(A) receptors can be co-purified from rat brain and exhibit a direct physical interaction as demonstrated by co-precipitation and Forster resonance energy transfer (FRET) analysis in a heterologous expression system. The brain-specific isoform neuroplastin-65 co-localizes with GABA(A) receptors as shown in brain sections as well as in neuronal cultures, and such complexes can either contain gephyrin or be devoid of gephyrin. Neuroplastin-65 specifically co-localizes with alpha1 or alpha2 but not with alpha3 subunits at GABAergic synapses. In addition, neuroplastin-65 also co-localizes with GABA(A) receptor alpha5 subunits at extra-synaptic sites. Down-regulation of neuroplastin-65 by shRNA causes a loss of GABA(A) receptor alpha2 subunits at GABAergic synapses. These results suggest that neuroplastin-65 can co-localize with a subset of GABA(A) receptor subtypes and might contribute to anchoring and/or confining GABA(A) receptors to particular synaptic or extra-synaptic sites, thus affecting receptor mobility and synaptic strength.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
positive regulation of protein localization  IMP 9835374 RGD 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
dendrite  IDA 9835374 RGD 
GABA-ergic synapse is_active_inIDA 9835374PMID:22389504SynGO 
inhibitory synapse  IDA 9835374 RGD 
synaptic membrane is_active_inIDA 9835374PMID:22389504SynGO 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein binding  IPINptn (Rattus norvegicus)9835374 RGD 
transmembrane transporter binding  IPIGabrb2 (Rattus norvegicus)9835374 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Gabrb2  (gamma-aminobutyric acid type A receptor subunit beta 2)
Nptn  (neuroplastin)


Additional Information