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Cis-Reporting System Monitors Intracellular Calcium Mobilization

larity to the dbd of Rel-family transcription factors.1 The NHR is about 300 amino acid residues in length and is located N-terminal to the dbd. Although the dbd sequences of different isoforms of NFAT proteins have distinct affinities, they bind to a consensus sequence of T(A)GGAAAAT(A/C).1,2 This site is present in many genes involved in immune responses, including interleukin-2 (IL-2), IL-4, IL-5, granular macrophage colony-stimulating factor (GM-CSF), IFN-g, and IL-13. In many cases, for DNA binding and transactivation, NFAT proteins cooperate with AP-1, which binds c-Jun/fos dimers. Complexes formed from cooperative binding of NFAT proteins, AP-1, and DNA are significantly more stable than complexes of NFAT and DNA alone.3,4

In resting cells, NFAT proteins are phosphorylated and reside in the cytoplasm. Stimuli that increase calcium mobilization result in the activation of NFAT proteins. The rapid dephosphorylation and translocation of NFAT proteins to the nucleus characterize activation; upon translocation, the dephosphorylated proteins show higher affinity for DNA. CsA or FK506 can block each step in the activation of NFAT proteins. Therefore, NFAT activation follows precisely the activation of calcineurin by increased free calcium levels in the cytoplasm.5,6 Researchers from diverse fields are interested in the NFAT family of transcription factors, which are potential targets for newer and safer immunosuppressive drugs.1 In addition, the activation of NFAT proteins involves various cellular signal transduction pathways, including calcium mobilization and MAP kinase pathways linked to T-cell receptors and Ras.1 To assist researchers probing the activity of NFAT proteins, Stratagene has developed a new PathDetect cis-reporter plasmid, the pNFAT-Luc reporter plasmid, containing the NFAT binding site from the human IL-2 gene.2,7-9
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