Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity
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- Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity
- Song, M; Kim, MJ; Ha, S; Park, JB; Ryu, SH; Suh, PG
- Issue Date
- KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
- EXPERIMENTAL AND MOLECULAR MEDICINE, v.37, no.3, pp.161 - 168
- Phospholipase C-gamma 1, 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-gamma 1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIN as the binding protein for the SH3 domain of PLC-gamma 1. SHIP1 was co-immunoprecipitated with PLC-gamma 1 and potentiated EGF-induced PLC-gamma 1 activation. However, inositol 5'-phosphatase activity of SHIN was not required for the potentiation of EGF-induced PLC-gamma 1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-gamma 1 activation without regards to its inositol 5'-phosphatase activity.
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