Stoichiometry and phosphoisotypes of hippocampal AMPA-type glutamate receptor phosphorylation.
Neuron
; 85(1): 60-67, 2015 Jan 07.
Article
em En
| MEDLINE
| ID: mdl-25533481
ABSTRACT
It has been proposed that the AMPAR phosphorylation regulates trafficking and channel activity, thereby playing an important role in synaptic plasticity. However, the actual stoichiometry of phosphorylation, information critical to understand the role of phosphorylation, is not known because of the lack of appropriate techniques for measurement. Here, using Phos-tag SDS-PAGE, we estimated the proportion of phosphorylated AMPAR subunit GluA1. The level of phosphorylated GluA1 at S831 and S845, two major sites implicated in AMPAR regulation, is almost negligible. Less than 1% of GluA1 is phosphorylated at S831 and less than 0.1% at S845. Considering the number of AMPAR at each synapse, the majority of synapses do not contain any phosphorylated AMPAR. Also, we did not see evidence of GluA1 dually phosphorylated at S831 and S845. Neuronal stimulation and learning increased phosphorylation, but the proportion was still low. Our results impel us to reconsider the mechanisms underlying synaptic plasticity.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Serina
/
Aprendizagem da Esquiva
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Receptores de AMPA
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Hipocampo
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Plasticidade Neuronal
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article