Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-γ1 and modulates EGF-induced PLC activity

Phospholipase C-γ1, 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-γ1 regulation is unclear. By pe...

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Bibliographic Details
Published in:Experimental & molecular medicine 2005, 37(3), , pp.161-168
Main Authors: 송민석, 김명종, 하상훈, 박종배, 류성호, 서판길
Format: Article
Language:Korean
Subjects:
생화학
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Summary:Phospholipase C-γ1, 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-γ1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIP1 as the binding protein for the SH3 domain of PLC-γ1. SHIP1 was co-immunoprecipitated with PLC-γ1 and potentiated EGF-induced PLC-γ1 activation. However, inositol 5'-phosphatase activity of SHIP1 was not required for the potentiation of EGF-induced PLC-γ1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-γ1 activation without regards to its inositol 5'-phosphatase activity. KCI Citation Count: 8
ISSN:1226-3613
2092-6413