A post-docking role for synaptobrevin in synaptic vesicle fusion.
Neuron
; 12(6): 1269-79, 1994 Jun.
Article
en En
| MEDLINE
| ID: mdl-8011337
ABSTRACT
We have used the squid giant synapse to determine the role of synaptobrevin, integral membrane proteins of small synaptic vesicles, in neurotransmitter release. The sequence of squid synaptobrevin, deduced by cDNA cloning, is 65%-68% identical to mammalian isoforms and includes the conserved cleavage site for tetanus and botulinum B toxins. Injection of either toxin into squid nerve terminals caused a slow, irreversible inhibition of release without affecting the Ca2+ signal which triggers release. Microinjection of a recombinant protein corresponding to the cytoplasmic domain of synaptobrevin produced a more rapid and reversible inhibition of release, whereas two smaller peptide fragments were without effect. Electron microscopy of tetanus-injected terminals revealed an increased number of both docked and undocked synaptic vesicles. These data indicate that synaptobrevin participates in neurotransmitter release at a step between vesicle docking and fusion.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Vesículas Sinápticas
/
Fusión de Membrana
/
Proteínas de la Membrana
/
Proteínas del Tejido Nervioso
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Neuron
Asunto de la revista:
NEUROLOGIA
Año:
1994
Tipo del documento:
Article