Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity
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- Title
- Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity
- Authors
- Song, M; Kim, MJ; Ha, S; Park, JB; Ryu, SH; Suh, PG
- Date Issued
- 2005-06-30
- Publisher
- KOREAN SOC MED BIOCHEMISTRY MOLECULAR
- Abstract
- 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/24483
- DOI
- 10.1038/emm.2005.22
- ISSN
- 1226-3613
- Article Type
- Article
- Citation
- EXPERIMENTAL AND MOLECULAR MEDICINE, vol. 37, no. 3, page. 161 - 168, 2005-06-30
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