Interaction of phospholipase C gamma 1 via its COOH-terminal SRC homology 2 domain with synaptojanin.
Biochem Biophys Res Commun
; 244(1): 62-7, 1998 Mar 06.
Article
em En
| MEDLINE
| ID: mdl-9514887
ABSTRACT
The role of the phospholipase C gamma 1 (PLC gamma 1) in signal transduction was investigated by characterizing its interactions with proteins that may represent components of a novel signalling pathway. A 145-kDa protein that binds SH2 domain of PLC gamma 1 was purified from rat brain. The sequence of peptide derived from the purified binding protein now identify it as synaptojanin, a nerve terminal protein that has been implicated in the endocytosis of fused synaptic vesicles and shown to be a member of the inositol polyphosphate 5-phosphatase family. We demonstrate here stable association of PLC gamma 1 with synaptojanin, a protein that not only binds carboxyl terminal SH2 domain of PLC gamma 1, but also inhibits PLC gamma 1 activity.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfolipases Tipo C
/
Monoéster Fosfórico Hidrolases
/
Domínios de Homologia de src
/
Isoenzimas
/
Proteínas do Tecido Nervoso
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1998
Tipo de documento:
Article