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Stable HeLa Luciferase Reporter Cell Lines Expressing GAL4 Fusion,,,Transactivators

s elaborate networks of signaling molecules (e.g., receptors, protein kinases, and phosphatases) organized in linear or parallel pathways.1,2 These signaling pathways receive diverse upstream signals that cause distinct downstream changes. Among the better-characterized signal transduction pathways are the cAMP-dependent protein kinase (PKA) pathway and the mitogen-activated protein kinase (MAPK) pathways. When activated by upstream signals, PKA or MAPK translocates into the nucleus and activates transcription factors, such as CREB and Elk1.3 Thus, the activation level of the transcription factors reflects the status of the respective kinases and upstream signaling molecules along the pathway.

To facilitate studies on the in vivo functions of gene products or extracellular stimuli, Stratagene developed the PathDetect trans-reporting systems using GAL4 fusion transactivators as pathway-specific sensors.4,5,6,7 In these systems, a fusion trans-activator plasmid that consists of the DNA binding domain of the yeast GAL4 (residues 1 to 147) protein8 and the activation domain of CREB, Elk1, or c-Jun is used to probe the activity of PKA, MAPK, and JNK, respectively.4-7,9,10 These fusion trans-activators bind to the promoter in the pFR-Luc reporter plasmid, which contains five direct repeats of the GAL4-binding element and controls luciferase expression.4 Either direct or indirect phosphorylation of the activation domain of a fusion trans-activator protein by an uncharacterized gene product activates transcription of the luciferase gene. Thus, expression levels of luciferase reflect the activation status of the respective kinases that define the signal transduction pathways.

To offer expanded capability for studying signal transduction and improved performance for adaptation to high-throughput applications, Stratagene has developed stable HeLa re
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