Synaptotagmin is endogenously phosphorylated by Ca2+/calmodulin protein kinase II in synaptic vesicles.
FEBS Lett
; 317(1-2): 85-8, 1993 Feb 08.
Article
em En
| MEDLINE
| ID: mdl-8381369
ABSTRACT
The cytoplasmic domain of synaptotagmin (a synaptic vesicle-specific protein) has a high degree of homology with the Ca(2+)-phospholipid binding domain of protein kinase C. The Ca(2+)-phospholipid binding activity of synaptotagmin has been implicated in the docking and fusion of synaptic vesicles with the presynaptic membrane during Ca(2+)-induced exocytosis. The protein sequence contains potential phosphorylation sites for various protein kinases which could modulate its binding activity. At present there is no clear evidence that the protein is endogenously phosphorylated in intact vesicles. Here it is reported that phospho-synaptotagmin was immunoprecipitated from endogenously phosphorylated synaptic vesicles. The conditions used indicate that synaptotagmin, as synapsin I, is phosphorylated by Ca2+/calmodulin-dependent protein kinase II.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Proteínas Quinases
/
Vesículas Sinápticas
/
Proteínas de Ligação ao Cálcio
/
Glicoproteínas de Membrana
/
Proteínas do Tecido Nervoso
Limite:
Animals
Idioma:
En
Ano de publicação:
1993
Tipo de documento:
Article