Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 17, Issue 5, Pages 2267-2277Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E05-10-0918
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Both phospholipase (PL) C-gamma 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-gamma 1 directly and activates Akt indirectly through phosphatidylinositol 3-kinase (PI3K). Many studies have shown that the PLC-gamma 1 pathway and PI3K-Akt pathway interact with each other. However, it is not known whether PLC-gamma 1 binds to Akt directly. In this communication, we identified a novel interaction between PLC-gamma 1 and Akt. We demonstrated that the interaction is mediated by the binding of PLC-gamma 1 Src homology (SH) 3 domain to Akt proline-rich motifs. We also provide a novel model to depict how the interaction between PLC-gamma 1 SH3 domain and Akt proline-rich motifs is dependent on EGF stimulation. In this model, phosphorylation of PLC-gamma 1 Y783 by EGF causes the conformational change of PLC-gamma 1 to allow the interaction of its SH3 domain with Akt proline-rich motifs. Furthermore, we showed that the interaction between PLC-gamma 1 and Akt resulted in the phosphorylation of PLC-gamma 1 S1248 by Akt. Finally, we showed that the interaction between PLC-gamma 1 and Akt enhanced EGF-stimulated cell motility.
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