Differential nuclear receptor signalling from DR4‐type response elements
Identifieur interne : 000935 ( Main/Exploration ); précédent : 000934; suivant : 000936Differential nuclear receptor signalling from DR4‐type response elements
Auteurs : Marcus Quack [Allemagne] ; Christian Frank [Finlande] ; Carsten Carlberg [Allemagne, Finlande]Source :
- Journal of Cellular Biochemistry [ 0730-2312 ] ; 2002.
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Abstract
Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.
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DOI: 10.1002/jcb.10247
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Cell. Biochem.</title><idno type="ISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="2002">2002</date><biblScope unit="volume">86</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="601">601</biblScope><biblScope unit="page" to="612">612</biblScope></imprint><idno type="ISSN">0730-2312</idno></series><idno type="istex">01C9C305B207DC8E1C9741284A6DAA2F01DC3A74</idno><idno type="DOI">10.1002/jcb.10247</idno><idno type="ArticleID">JCB10247</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0730-2312</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>complexes</term><term>heterodimeric nuclear receptor</term><term>liver X receptor</term><term>response elements</term><term>retinoid X receptor</term><term>thyroid hormone receptor</term><term>transcriptional regulation</term><term>vitamin D receptor</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Finlande</li></country><region><li>District de Düsseldorf</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Düsseldorf</li></settlement></list><tree><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Quack, Marcus" sort="Quack, Marcus" uniqKey="Quack M" first="Marcus" last="Quack">Marcus Quack</name></region><name sortKey="Carlberg, Carsten" sort="Carlberg, Carsten" uniqKey="Carlberg C" first="Carsten" last="Carlberg">Carsten Carlberg</name><name sortKey="Quack, Marcus" sort="Quack, Marcus" uniqKey="Quack M" first="Marcus" last="Quack">Marcus Quack</name></country><country name="Finlande"><noRegion><name sortKey="Frank, Christian" sort="Frank, Christian" uniqKey="Frank C" first="Christian" last="Frank">Christian Frank</name></noRegion><name sortKey="Carlberg, Carsten" sort="Carlberg, Carsten" uniqKey="Carlberg C" first="Carsten" last="Carlberg">Carsten Carlberg</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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