Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity
Experimental & Molecular Medicine
;
: 161-168, 2005.
Article
in English
| WPRIM
| ID: wpr-201947
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Type C Phospholipases
/
Protein Binding
/
Molecular Sequence Data
/
Signal Transduction
/
Inositol 1,4,5-Trisphosphate
/
Chlorocebus aethiops
/
Amino Acid Sequence
/
Phosphoric Monoester Hydrolases
/
Src Homology Domains
/
COS Cells
Type of study:
Prognostic study
Limits:
Animals
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2005
Type:
Article
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