| First Author | Song M | Year | 2005 |
| Journal | Exp Mol Med | Volume | 37 |
| Issue | 3 | Pages | 161-8 |
| PubMed ID | 16000869 | Mgi Jnum | J:243541 |
| Mgi Id | MGI:5908793 | Doi | 10.1038/emm.2005.22 |
| Citation | Song M, et al. (2005) Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity. Exp Mol Med 37(3):161-8 |
| abstractText | 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. |
