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Cell Biology - The Scientist - Magazine of the Life Sciences

Cell Biology - The Scientist - Magazine of the Life Sciences S.A. Kliewer, L. Umesono, D.I. Mangelsdorf, R.M. Evans, "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone, and vitamin D signalling," Nature, 355:446-9, 1992. Steven Kliewer (The Salk Institute, La Jolla, Calif.): "Vitamin D, thyroid hormone, and all-trans retinoic acid are essential cofactors in development, differentiation, and homeostasis. The effects of these endocrine signals on target gene expression are mediated through nuclear hormone receptors (VDR, TR, and RAR), which function as ligand-activated transcriptional regulators by binding to specific DNA sequences, termed hormone response elements (HREs). Work from several laboratories had indicated that VDR, TR, and RAR require auxiliary nuclear factors for high- affinity binding to their cognate HREs. However, the identity of these factors was unknown. In addressing this issue, we have shown that, surprisingly, each of these receptors binds cooperatively to its HRE through the formation of a heterodimer with the retinoid X receptor (RXR), itself a receptor for the novel hormone 9-cis retinoic acid. More recently, we showed that RXR forms an additional heterodimer with peroxisome proliferator- activated receptor, a receptor activated by fatty acids and hypolipidemic drugs such as clofibric acid (S.A. Kliewer, et al., Nature, 358:771-4, 1992). Thus, RXR serves a http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Scientist The Scientist

Cell Biology - The Scientist - Magazine of the Life Sciences

The Scientist , Volume 7 (8): 16 – Apr 19, 1993

Cell Biology - The Scientist - Magazine of the Life Sciences

The Scientist , Volume 7 (8): 16 – Apr 19, 1993

Abstract

S.A. Kliewer, L. Umesono, D.I. Mangelsdorf, R.M. Evans, "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone, and vitamin D signalling," Nature, 355:446-9, 1992. Steven Kliewer (The Salk Institute, La Jolla, Calif.): "Vitamin D, thyroid hormone, and all-trans retinoic acid are essential cofactors in development, differentiation, and homeostasis. The effects of these endocrine signals on target gene expression are mediated through nuclear hormone receptors (VDR, TR, and RAR), which function as ligand-activated transcriptional regulators by binding to specific DNA sequences, termed hormone response elements (HREs). Work from several laboratories had indicated that VDR, TR, and RAR require auxiliary nuclear factors for high- affinity binding to their cognate HREs. However, the identity of these factors was unknown. In addressing this issue, we have shown that, surprisingly, each of these receptors binds cooperatively to its HRE through the formation of a heterodimer with the retinoid X receptor (RXR), itself a receptor for the novel hormone 9-cis retinoic acid. More recently, we showed that RXR forms an additional heterodimer with peroxisome proliferator- activated receptor, a receptor activated by fatty acids and hypolipidemic drugs such as clofibric acid (S.A. Kliewer, et al., Nature, 358:771-4, 1992). Thus, RXR serves a

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The Scientist
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© 1986-2010 The Scientist
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1759-796X
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Abstract

S.A. Kliewer, L. Umesono, D.I. Mangelsdorf, R.M. Evans, "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone, and vitamin D signalling," Nature, 355:446-9, 1992. Steven Kliewer (The Salk Institute, La Jolla, Calif.): "Vitamin D, thyroid hormone, and all-trans retinoic acid are essential cofactors in development, differentiation, and homeostasis. The effects of these endocrine signals on target gene expression are mediated through nuclear hormone receptors (VDR, TR, and RAR), which function as ligand-activated transcriptional regulators by binding to specific DNA sequences, termed hormone response elements (HREs). Work from several laboratories had indicated that VDR, TR, and RAR require auxiliary nuclear factors for high- affinity binding to their cognate HREs. However, the identity of these factors was unknown. In addressing this issue, we have shown that, surprisingly, each of these receptors binds cooperatively to its HRE through the formation of a heterodimer with the retinoid X receptor (RXR), itself a receptor for the novel hormone 9-cis retinoic acid. More recently, we showed that RXR forms an additional heterodimer with peroxisome proliferator- activated receptor, a receptor activated by fatty acids and hypolipidemic drugs such as clofibric acid (S.A. Kliewer, et al., Nature, 358:771-4, 1992). Thus, RXR serves a

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The ScientistThe Scientist

Published: Apr 19, 1993

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