RGD Reference Report - NSF binding to GluR2 regulates synaptic transmission. - Rat Genome Database
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NSF binding to GluR2 regulates synaptic transmission.

Authors: Nishimune, A  Isaac, JT  Molnar, E  Noel, J  Nash, SR  Tagaya, M  Collingridge, GL  Nakanishi, S  Henley, JM 
Citation: Nishimune A, etal., Neuron. 1998 Jul;21(1):87-97.
RGD ID: 8553822
Pubmed: (View Article at PubMed) PMID:9697854

Here, we show that N-ethylmaleimide-sensitive fusion protein (NSF) interacts directly and selectively with the intracellular C-terminal domain of the GluR2 subunit of AMPA receptors. The interaction requires all three domains of NSF but occurs between residues Lys-844 and Gln-853 of rat GluR2, with Asn-851 playing a critical role. Loading of decapeptides corresponding to the NSF-binding domain of GluR2 into rat hippocampal CA1 pyramidal neurons results in a marked, progressive decrement of AMPA receptor-mediated synaptic transmission. This reduction in synaptic transmission was also observed when an anti-NSF monoclonal antibody (mAb) was loaded into CA1 neurons. These results demonstrate a previously unsuspected direct interaction in the postsynaptic neuron between two major proteins involved in synaptic transmission and suggest a rapid NSF-dependent modulation of AMPA receptor function.


Gene Ontology Annotations    

Biological Process

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Gria2  (glutamate ionotropic receptor AMPA type subunit 2)
Gria3  (glutamate ionotropic receptor AMPA type subunit 3)
Grip2  (glutamate receptor interacting protein 2)
Nsf  (N-ethylmaleimide sensitive factor, vesicle fusing ATPase)

Additional Information