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Molecular Endocrinology 15 (4): 501-511
Copyright © 2001 by The Endocrine Society

Regulation of Glucocorticoid Receptor Activity by 14–3-3-Dependent Intracellular Relocalization of the Corepressor RIP140

Johanna Zilliacus, Elin Holter, Hideki Wakui1, Hiroshi Tazawa, Eckardt Treuter and Jan-Åke Gustafsson

Department of Medical Nutrition (J.Z., H.W., H.T., J.-A.G.) and Department of Biosciences (E.H., E.T., J.-A.G.) Karolinska Institutet Novum, S-141 86 Huddinge, Sweden

Proteins belonging to the 14–3-3 family interact with various regulatory proteins involved in cellular signaling, cell cycle regulation, or apoptosis. 14–3-3 proteins have been suggested to act by regulating the cytoplasmic/nuclear localization of their target proteins or by acting as molecular scaffolds or chaperones. We have previously shown that overexpression of 14–3-3 enhances the transcriptional activity of the glucocorticoid receptor (GR), which is a member of the nuclear receptor family. In this study, we show that 14–3-3 interacts with the nuclear receptor corepressor RIP140. In transfection assays, RIP140 antagonizes 14–3-3- enhanced GR transactivation. Using colocalization studies we demonstrate that 14–3-3 can export RIP140 out of the nucleus and, interestingly, can also change its intranuclear localization. Moreover, we also observed that 14–3-3 can bind various other nuclear receptors and cofactors. In summary, our findings suggest that 14–3-3-mediated intracellular relocalization of the GR corepressor RIP140 might be a novel mechanism to enhance glucocorticoid responsiveness of target genes. They furthermore indicate a more general role for 14–3-3 protein by influencing the nuclear availability of nuclear receptor-associated cofactors.




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