Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity
Experimental & Molecular Medicine
; : 161-168, 2005.
Artigo
em Inglês
| WPRIM (Pacífico Ocidental)
| ID: wpr-201947
Biblioteca responsável:
WPRO
ABSTRACT
Phospholipase C-gamma1, containing two SH2 and one SH3 domains which participate in the interaction between signaling molecules, plays a significant role in the growth factor-induced signal transduction. However, the role of the SH domains in the growth factor-induced PLC-gamma1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIP1 as the binding protein for the SH3 domain of PLC-gamma1. SHIP1 was co-immunoprecipitated with PLC-gamma1 and potentiated EGF-induced PLC-gamma1 activation. However, inositol 5'-phosphatase activity of SHIP1 was not required for the potentiation of EGF-induced PLC-gamma1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-gamma1 activation without regards to its inositol 5'-phosphatase activity.
Texto completo:
Disponível
Base de dados:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fosfolipases Tipo C
/
Ligação Proteica
/
Dados de Sequência Molecular
/
Transdução de Sinais
/
Inositol 1,4,5-Trifosfato
/
Chlorocebus aethiops
/
Sequência de Aminoácidos
/
Monoéster Fosfórico Hidrolases
/
Domínios de Homologia de src
/
Células COS
Tipo de estudo:
Estudo prognóstico
Limite:
Animais
Idioma:
Inglês
Revista:
Experimental & Molecular Medicine
Ano de publicação:
2005
Tipo de documento:
Artigo