| Literature DB >> 28470379 |
Amit K Dash1, Ashutosh S Yende1, Rakesh K Tyagi2.
Abstract
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.Entities:
Keywords: CAR; GFP; PXR; RFP; RXRα; Subcellular localization
Mesh:
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Year: 2017 PMID: 28470379 DOI: 10.1007/s10895-017-2109-z
Source DB: PubMed Journal: J Fluoresc ISSN: 1053-0509 Impact factor: 2.217