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Assess the In Vivo Activation of Signal Transduction Pathways with,,,PathDetect Reporting Systems

of an unrelated plasmid (pBluescript plasmid). The pFC2-dbd plasmid, which expresses the GAL4 DNA binding domain but lacks an activation domain, was used as the negative control. Transfection procedure, maintenance of transfected cells, cell lysate preparation, and luciferase assay have been described previously.5

The pFR-Luc plasmid, the pFA2-cJun fusion trans-activator plasmid, and the pFC-MEKK control plasmid were cotransfected into HeLa cells. The pFA2-Jun fusion trans-activator plasmid is specific for the c-Jun N-terminal kinase10,16 (JNK) signaling pathway and the pFC-MEKK control plasmid constitutively expresses MEKK kinase17. The MEKK protein, a known JNK activator, increased the expression of the luciferase gene by more than 100-fold (Figure 2A), indicating activation of the GAL4-cJun fusion protein.5,10 The pFC2-dbd plasmid could not be activated by overexpression of the MEKK protein.

The specificity of the pFA2-CREB fusion activator plasmid is shown in Figure 2B. Cyclic AMP-dependent protein kinase (PKA) is a known activator of the CREB protein, and the pFC-PKA plasmid expresses this active kinase.14,18 When the pFA2-CREB plasmid was cotransfected with the pFC-PKA plasmid and the pFR-Luc reporter plasmid, a 100-fold increase in luciferase expression was seen. As expected, cotransfection of the pFR-Luc and pFC-PKA plasmids with the pFC2-dbd plasmid yielded only background levels of luciferase activity.

In a similar fashion, the specificity of the pFA2-Elk1 fusion activator plasmid is demonstrated (Figure 2C). Since the MEK1 protein is a known upstream activator of the Elk1
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