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Article: Heterodimeric interaction of the retinoic acid and thyroid hormone receptors in transcriptional regulation on the γF-crystallin everted retinoic acid response element

TitleHeterodimeric interaction of the retinoic acid and thyroid hormone receptors in transcriptional regulation on the γF-crystallin everted retinoic acid response element
Authors
Issue Date1994
PublisherEndocrine Society. The Journal's web site is located at http://mend.endojournals.org/
Citation
Molecular Endocrinology, 1994, v. 8 n. 11, p. 1494-1506 How to Cite?
AbstractPreviously, we have identified a hormone response element (γF-HRE) composed of an everted repeat of the half-site (A/G)GGTCA motif separated by 8 base pairs that mediates retinoic acid (RA) activation of the γF- crystallin promoter. Here, we report that this element is bound by the thyroid hormone (T 3) receptor in the form of heterodimers with either the retinoid X receptor (RXR) or the retinoic acid receptor (RAR). The T 3R/RXR heterodimer binds to this element with high affinity but the transcriptional activity of the T 3 receptor on this element is effectively antagonized by RARα. Thus, RARα exerts a dominant effect on the γF-HRE-everted repeat by mediating both RA activation and preventing T 3 response. Although RAR/T 3R heterodimers bind to the γF-HRE, they do not appear to be involved in transcriptional regulation since they bind with low affinity, and their ability to bind DNA is dramatically decreased by T 3. Repression requires the DNA- and ligand-binding domains of RARα and is consistent with a competitive DNA binding model of repression. However, in vitro binding studies indicate that RAR/RXR heterodimers form less stable interactions with the γF-HRE compared with T 3R/RXR heterodimers; this suggests that in vivo the binding affinity of RAR/RXR heterodimers may be enhanced by accessory factors.
Persistent Identifierhttp://hdl.handle.net/10722/133882
ISSN
2015 Impact Factor: 3.432
2015 SCImago Journal Rankings: 2.195
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTini, Men_HK
dc.contributor.authorTsui, LCen_HK
dc.contributor.authorGiguère, Ven_HK
dc.date.accessioned2011-06-03T03:31:05Z-
dc.date.available2011-06-03T03:31:05Z-
dc.date.issued1994en_HK
dc.identifier.citationMolecular Endocrinology, 1994, v. 8 n. 11, p. 1494-1506en_HK
dc.identifier.issn0888-8809en_HK
dc.identifier.urihttp://hdl.handle.net/10722/133882-
dc.description.abstractPreviously, we have identified a hormone response element (γF-HRE) composed of an everted repeat of the half-site (A/G)GGTCA motif separated by 8 base pairs that mediates retinoic acid (RA) activation of the γF- crystallin promoter. Here, we report that this element is bound by the thyroid hormone (T 3) receptor in the form of heterodimers with either the retinoid X receptor (RXR) or the retinoic acid receptor (RAR). The T 3R/RXR heterodimer binds to this element with high affinity but the transcriptional activity of the T 3 receptor on this element is effectively antagonized by RARα. Thus, RARα exerts a dominant effect on the γF-HRE-everted repeat by mediating both RA activation and preventing T 3 response. Although RAR/T 3R heterodimers bind to the γF-HRE, they do not appear to be involved in transcriptional regulation since they bind with low affinity, and their ability to bind DNA is dramatically decreased by T 3. Repression requires the DNA- and ligand-binding domains of RARα and is consistent with a competitive DNA binding model of repression. However, in vitro binding studies indicate that RAR/RXR heterodimers form less stable interactions with the γF-HRE compared with T 3R/RXR heterodimers; this suggests that in vivo the binding affinity of RAR/RXR heterodimers may be enhanced by accessory factors.en_HK
dc.languageeng-
dc.publisherEndocrine Society. The Journal's web site is located at http://mend.endojournals.org/en_HK
dc.relation.ispartofMolecular Endocrinologyen_HK
dc.subject.meshCrystallins - antagonists and inhibitors - biosynthesis - genetics-
dc.subject.meshPromoter Regions, Genetic-
dc.subject.meshReceptors, Retinoic Acid - metabolism-
dc.subject.meshReceptors, Thyroid Hormone - metabolism-
dc.subject.meshTretinoin - metabolism - pharmacology-
dc.titleHeterodimeric interaction of the retinoic acid and thyroid hormone receptors in transcriptional regulation on the γF-crystallin everted retinoic acid response elementen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0888-8809&volume=8&issue=11&spage=1494&epage=1506&date=1994&atitle=Heterodimeric+interaction+of+the+retinoic+acid+and+thyroid+hormone+receptors+in+transcriptional+regulation+on+the+gamma+F-crystallin+everted+retinoic+acid+response+element-
dc.identifier.emailTsui, LC: tsuilc@hkucc.hku.hken_HK
dc.identifier.authorityTsui, LC=rp00058en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1210/me.8.11.1494en_HK
dc.identifier.pmid7877618-
dc.identifier.scopuseid_2-s2.0-0027946663en_HK
dc.identifier.hkuros121000-
dc.identifier.volume8en_HK
dc.identifier.issue11en_HK
dc.identifier.spage1494en_HK
dc.identifier.epage1506en_HK
dc.identifier.isiWOS:A1994PU43200007-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridTini, M=55409977200en_HK
dc.identifier.scopusauthoridTsui, LC=7102754167en_HK
dc.identifier.scopusauthoridGiguère, V=7006252444en_HK

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