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In Vivo Signal Transduction Pathway Reporting Systems

each fusion activator plasmid, known activators and nonactivators were cotransfected into HeLa cells with the pFR-Luc reporter plasmid. Cotransfections were performed using standard lipofection methods, and lysates were prepared and assayed for luciferase activity. The pFR-Luc plasmid was cotransfected into HeLa cells together with the fusion activator plasmid specific for the JNK signaling pathway ((pFA-cJun) and the pFC-MEKK control plasmid (figure 3, panel A). The MEKK protein, a known JNK activator, increased the expression of the luciferase gene by more than 100 fold (figure 3, panel A), indicating activation of the c-Jun transactivator fusion protein.7,15 The pFC-dbd plasmid, which expresses the GAL4 DNA binding domain only and no activation domain, could not be activated by overexpression of the MEKK protein. A mutated form of the c-Jun transactivator fusion protein, which had alanine residues substituted for serine 63 and 73 in c-Jun, could not be activated by MEKK (data not shown).

In a similar fashion, the specificity of the pFA-Elk1 fusion activator plasmid was also demonstrated (figure 3, panel B). The ternary complex factor Elk1 is phosphorylated and activated by MAPK.10,11 The MEKK and MEK1 proteins are both known activators of the Elk1 protein. Cotransfection of the pFA-Elk1 vector with pFC-MEK1 vector resulted in 50-fold increased expression of luciferase, whereas cotransfection with pFC-MEKK vector resulted in 200-fold increased expression of luciferase. These data are consistent with reports that both MEK1 and MEKK proteins are known activators of the MAPK pathway. 16-18

The specificity of the pFA-CREB fusion activato
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