Molecular functions of the TLE tetramerization domain in Wnt target gene repression. (4th March 2014)

• Record Type: Journal Article
• Authors: Chodaparambil, Jayanth V; Pate, Kira T; Hepler, Margretta R D; Tsai, Becky P; Muthurajan, Uma M; Luger, Karolin; Waterman, Marian L; Weis, William I
• Is Part Of: EMBO journal. Volume 33:Number 7(2014)
• Page Start: 719
• Page End: 731
• Publication Date: 2014-03-04
• Subjects: Molecular biology -- Periodicals; 572.805
• DOI: 10.1002/embj.201387188
• Languages: English
• ISSNs: 0261-4189

Abstract

<abstract abstract-type="synopsis" xml:lang="en" id="embj201387188-abs-0002"> <title>Synopsis</title> <p> <boxed-text content-type="graphic" id="embj201387188-blkfxd-0011" position="anchor" orientation="portrait"> <graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg5279r25t" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /> </boxed-text> </p> <p>Bill Weis and colleagues present an unusual tetramer fold for the N‐terminal domain of the Groucho/TLE1 repressor. Their functional results propose chromatin binding, rather than competition for TCF as mechanism for Wnt‐target gene repression.</p> <p> <list id="embj201387188-list-0001" list-type="bullet"> <list-item> <p>The N‐terminal tetramerization domain of the transcriptional co‐repressor TLE1 forms an extended, interdigitated dimer of dimers</p> </list-item> <list-item> <p>TLE1 binds the repressive TCF3 and TCF4 proteins more strongly than the activating TCF1 and LEF1 proteins</p> </list-item> <list-item> <p>There is no direct competition between TLE and ß‐catenin for TCF/LEF binding, suggesting that other factors mediate the switch between repression and activation of Wnt target genes</p> </list-item> <list-item> <p>The TLE N‐terminal domain can bind chromatin through its interaction with K20 methylated H4 tails.</p> </list-item> </list> </p> </abstract>