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Polarity-specific activities of retinoic acid receptors determined by a co-repressor.
University of California, San Diego, USA.
University of California, San Diego, USA.ORCID iD: 0000-0003-3927-4394
University of California, San Diego, USA.
Dana Farber Cancer Institute, Boston, Massachusetts, USA .
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1995 (English)In: Nature, ISSN 0028-0836, Vol. 377, no 6548, 451-454 p.Article in journal (Refereed) Published
Abstract [en]

Retinoic acid receptors (RARs) and retinoid-X receptors (RXRs) activate or repress transcription by binding as heterodimers to DNA-response elements that generally consist of two direct repeat half-sites of consensus sequence AGGTCA. On response elements consisting of direct repeats spaced by five base pairs (DR + 5 elements), RAR/RXR heterodimers activate transcription in response to RAR-specific ligands, such as all-trans-retinoic acid (RA). In contrast, on elements consisting of direct repeats spaced by one base pair (DR + 1 elements), RAR/RXR heterodimers exhibit little or no response to activating ligands and repress RXR-dependent transcription. Here we show that ligand-dependent transactivation by RAR on DR + 5 elements requires the dissociation of a new nuclear receptor co-repressor, N-CoR, and recruitment of the putative co-activators p140 and p160. Surprisingly, on DR + 1 elements, N-CoR remains associated with RAR/RXR heterodimers even in the presence of RAR ligands, resulting in constitutive repression. These observations indicate that DNA-response elements can allosterically regulate RAR-co-repressor interactions to determine positive or negative regulation of gene expression.

Place, publisher, year, edition, pages
Nature Publishing Group, 1995. Vol. 377, no 6548, 451-454 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-87599DOI: 10.1038/377451a0ISI: A1995RY19000056PubMedID: 7566126OAI: diva2:589566
Available from: 2013-01-18 Created: 2013-01-18 Last updated: 2013-10-22

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Söderström, Mats
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