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Novel Application of Red Fluorescent Protein (DsRed-Express) for the Study of Functional Dynamics of Nuclear Receptors.
Journal of Fluorescence 2017 July
Arrivals of fluorescent proteins have revolutionized the way we do research in the areas of molecular cell biology. In the present study, we have successfully exploited the multimer-forming property of Red Fluorescent Protein (RFP) in living cells to preferentially shift the unliganded nuclear receptors from the nuclear to the cytoplasmic compartment. Subsequently, these cytoplasmic-shifted unliganded receptors could be induced to translocate into the nucleus by their ligands. Though the multimerization of RFP as a protein-tag is viewed as a disadvantage, we have exploited and projected this property towards novel applications in validating the clinical drugs, herbal compounds, metabolic disruptors etc. Such cytoplasmic shifted transcription factors can offer a unique opportunity to study receptor-ligand interactions and functional dynamics by analyzing ligand-mediated receptor translocation from cytoplasmic compartment to the nucleus of living cells.
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