Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity.
- Author:
Minseok SONG
1
;
Myung Jong KIM
;
Sanghoon HA
;
Jong Bae PARK
;
Sung Ho RYU
;
Pann Ghill SUH
Author Information
1. Department of Life Science, Division of Molecular and Life Science, Postech Biotech Center, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea. pgs@postech.ac.kr
- Publication Type:Original Article
- Keywords:
epidermal growth factor;
phospholipase C-gamma1;
SH2 domain-containing inositol 5'-phosphatase;
SH3 domain
- MeSH:
Adaptor Proteins, Signal Transducing;
Amino Acid Sequence;
Animals;
COS Cells/enzymology;
Cercopithecus aethiops;
Enzyme Activation;
Epidermal Growth Factor/*pharmacology;
Immunoprecipitation;
Inositol 1,4,5-Trisphosphate/metabolism;
Molecular Sequence Data;
Phospholipase C/chemistry/*metabolism;
Phosphoric Monoester Hydrolases/chemistry/*metabolism;
Protein Binding;
Signal Transduction;
src Homology Domains/*physiology
- From:Experimental & Molecular Medicine
2005;37(3):161-168
- CountryRepublic of Korea
- Language:English
-
Abstract:
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.
