NSF binding to GluR2 regulates synaptic transmission.
Neuron
; 21(1): 87-97, 1998 Jul.
Article
em En
| MEDLINE
| ID: mdl-9697854
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores de Glutamato
/
Transmissão Sináptica
/
Proteínas de Transporte Vesicular
Limite:
Animals
Idioma:
En
Ano de publicação:
1998
Tipo de documento:
Article