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10.1002/embj.201387188 http://scihub22266oqcxt.onion/10.1002/embj.201387188 C4000089!4000089!24596249     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2014 ; 33 (7): 719-31 Nephropedia Template TP {{tp|p=24596249|t=2014. Molecular functions of the TLE tetramerization domain in Wnt target gene repression |pdf=|usr=}}{{24596249}} gab.com Text Molecular functions of the TLE tetramerization domain in Wnt target gene repression JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=24596249 #FOAvip Wnt signaling activates target genes by promoting association of the co-activator ?-catenin with TCF/LEF transcription factors. In the absence of ?-catenin, target genes are silenced by TCF-mediated recruitment of TLE/Groucho proteins, but the molecular basis for TLE/TCF-dependent repression is unclear. We describe the unusual three-dimensional structure of the N-terminal Q domain of TLE1 that mediates tetramerization and binds to TCFs. We find that differences in repression potential of TCF/LEFs correlates with their affinities for TLE-Q, rather than direct competition between ?-catenin and TLE for TCFs as part of an activation?repression switch. Structure-based mutation of the TLE tetramer interface shows that dimers cannot mediate repression, even though they bind to TCFs with the same affinity as tetramers. Furthermore, the TLE Q tetramer, not the dimer, binds to chromatin, specifically to K20 methylated histone H4 tails, suggesting that the TCF/TLE tetramer complex promotes structural transitions of chromatin to mediate repression. Twit Text FOAVip Molecular functions of the TLE tetramerization domain in Wnt target gene repression ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=24596249 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24596249 #FOAvip English Wikipedia <ref>{{Cite pmid|24596249}}</ref> Molecular functions of the TLE tetramerization domain in Wnt target gene repression #MMPMID24596249 Chodaparambil JV; Pate KT; Hepler MRD; Tsai BP; Muthurajan UM; Luger K; Waterman ML; Weis WI EMBO J 2014[Apr]; 33 (7): 719-31 PMID24596249show ga Wnt signaling activates target genes by promoting association of the co-activator ?-catenin with TCF/LEF transcription factors. In the absence of ?-catenin, target genes are silenced by TCF-mediated recruitment of TLE/Groucho proteins, but the molecular basis for TLE/TCF-dependent repression is unclear. We describe the unusual three-dimensional structure of the N-terminal Q domain of TLE1 that mediates tetramerization and binds to TCFs. We find that differences in repression potential of TCF/LEFs correlates with their affinities for TLE-Q, rather than direct competition between ?-catenin and TLE for TCFs as part of an activation?repression switch. Structure-based mutation of the TLE tetramer interface shows that dimers cannot mediate repression, even though they bind to TCFs with the same affinity as tetramers. Furthermore, the TLE Q tetramer, not the dimer, binds to chromatin, specifically to K20 methylated histone H4 tails, suggesting that the TCF/TLE tetramer complex promotes structural transitions of chromatin to mediate repression. äMolecular functions of the TLE tetramerization domain in Wnt target ge(epmc).pdf DeepDyve Pubget Overpricing