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A more recent version of this article appeared on May 1, 2006
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Submitted on October 4, 2005
Revised on January 27, 2006
Accepted on February 27, 2006
1 in Response to EGF
Department of Cell Biology and Signal Transduction Research Group, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
Monitoring Editor: Ben Margolis
Both Phospholipase C-
1 (PLC-1) and Akt (Protein kinase B, PKB) are signaling proteins that play significant roles in the intracellular signaling mechanism utilized by receptor tyrosine kinases (RTKs) including epidermal growth factor (EGF) receptor (EGFR). EGFR activates PLC-1 directly and activates Akt indirectly through phosphatidylinositol 3-kinase (PI3K). Many data have shown that PLC-1 pathway and PI3K-Akt pathway interact each other. However, it is not known whether PLC-1 binds to Akt directly. In this communication, we identified a novel interaction between PLC-1 and Akt. We demonstrated that the interaction is mediated by the binding of PLC-1 SH3 domain to Akt proline rich motifs. We also provide a novel model to depict how the interaction between PLC-1 SH3 domain and Akt proline rich motifs is dependent on EGF stimulation. In this model, phosphorylation of PLC-1 Y783 by EGF causes the conformational change of PLC-1 to allow the interaction of its SH3 domain with Akt proline rich motifs. Furthermore, we showed that the interaction between PLC-1 and Akt resulted in the phosphorylation of PLC-1 S1248 by Akt. Finally we showed that the interaction between PLC-1 and Akt enhanced EGF-stimulated cell motility.
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