Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-[gamma]1 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 2005-06, Vol.37 (3), p.161
Main Authors: Song, Minseok, Kim, Myung Jong, Ha, Sanghoon, Park, Jong Bae, Ryu, Sung Ho, Suh, Pann-ghill
Format: Article
Language:English
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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.
ISSN:1226-3613
2092-6413
DOI:10.1038/emm.2005.22