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Vol. 17, Issue 5, 2267-2277, May 2006

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Akt Binds to and Phosphorylates Phospholipase C-1 in Response to Epidermal Growth Factor

Department of Cell Biology and Signal Transduction Research Group, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Submitted October 4, 2005; Revised January 27, 2006; Accepted February 27, 2006
Monitoring Editor: Ben Margolis

Both phospholipase (PL) C-1 and Akt (protein kinase B; PKB) are signaling proteins that play significant roles in the intracellular signaling mechanism used by receptor tyrosine kinases, including epidermal growth factor (EGF) receptor (EGFR). EGFR activates PLC-1 directly and activates Akt indirectly through phosphatidylinositol 3-kinase (PI3K). Many studies have shown that the PLC-1 pathway and PI3K–Akt pathway interact with 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 Src homology (SH) 3 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.

Address correspondence to: Zhixiang Wang (zhixiang.wang{at}ualberta.ca).

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