Exp Mol Med.  2005 Jun;37(3):161-168.

Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity

• Song M
• Kim MJ
• Ha S
• Park JB
• Ryu SH
• Suh PG

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.

Keyword

epidermal growth factor; phospholipase C-gamma1; SH2 domain-containing inositol 5'-phosphatase; SH3 domain

MeSH Terms

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