Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin.
Neuron
; 27(2): 301-12, 2000 Aug.
Article
em En
| MEDLINE
| ID: mdl-10985350
ABSTRACT
Coordination between sequential steps in synaptic vesicle endocytosis, including clathrin coat formation, fission, and uncoating, appears to involve proteinprotein interactions. Here, we show that compounds that disrupt interactions of the SH3 domain of endophilin with dynamin and synaptojanin impair synaptic vesicle endocytosis in a living synapse. Two distinct endocytic intermediates accumulated. Free clathrin-coated vesicles were induced by a peptide-blocking endophilin's SH3 domain and by antibodies to the proline-rich domain (PRD) of synaptojanin. Invaginated clathrin-coated pits were induced by the same peptide and by the SH3 domain of endophilin. We suggest that the SH3 domain of endophilin participates in both fission and uncoating and that it may be a key component of a molecular switch that couples the fission reaction to uncoating.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Vesículas Sinápticas
/
Proteínas de Transporte
/
Clatrina
/
Invaginações Revestidas da Membrana Celular
/
Monoéster Fosfórico Hidrolases
/
Domínios de Homologia de src
/
Proteínas Adaptadoras de Transdução de Sinal
/
Proteínas do Tecido Nervoso
Limite:
Animals
Idioma:
En
Revista:
Neuron
Ano de publicação:
2000
Tipo de documento:
Article