Block of kainate receptor desensitization uncovers a key trafficking checkpoint.
Neuron
; 52(6): 1037-46, 2006 Dec 21.
Article
em En
| MEDLINE
| ID: mdl-17178406
ABSTRACT
A prominent feature of ionotropic glutamate receptors from the AMPA and kainate subtypes is their profound desensitization in response to glutamate-a process thought to protect the neuron from overexcitation. In AMPA receptors, it is well established that desensitization results from rearrangements of the interface formed between agonist-binding domains of adjacent subunits; however, it is unclear how this mechanism applies to kainate receptors. Here we show that stabilization of the binding domain dimer by the generation of intermolecular disulfide bonds apparently blocked desensitization of the kainate receptor GluR6. This result establishes a common desensitization mechanism in both AMPA and kainate receptors. Surprisingly, however, surface expression of these nondesensitizing mutants was drastically reduced and did not depend on channel activity. Therefore, in addition to its role at the synapse, we now propose an intracellular role for desensitization in controlling maturation and trafficking of glutamate receptors.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores de Ácido Caínico
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Neuron
Assunto da revista:
NEUROLOGIA
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Israel