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10.1038/s41598-017-02219-9

http://scihub22266oqcxt.onion/10.1038/s41598-017-02219-9
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C5435683!5435683!28515457
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suck abstract from ncbi


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pmid28515457      Sci+Rep 2017 ; 7 (ä): ä
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  • Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex #MMPMID28515457
  • Kaan HYK; Chan SW; Tan SKJ; Guo F; Lim CJ; Hong W; Song H
  • Sci Rep 2017[]; 7 (ä): ä PMID28515457show ga
  • The Hippo pathway is a tumor suppressor pathway that is implicated in the regulation of organ size. The pathway has three components: the upstream regulatory factors, the kinase core, and the downstream transcriptional machinery, which consists of YAP, TAZ (transcription co-activators) and TEAD (transcription factor). Formation of YAP/TAZ-TEAD complexes leads to the transcription of growth-promoting genes. Herein, we report the crystal structure of TAZ-TEAD4 complex, which reveals two binding modes. The first is similar to the published YAP-TEAD structure. The second is a unique binding mode, whereby two molecules of TAZ bind to and bridge two molecules of TEAD4. We validated the latter using cross-linking and multi-angle light scattering. Using siRNA, we showed that TAZ knockdown leads to a decrease in TEAD4 dimerization. Lastly, results from luciferase assays, using YAP/TAZ transfected or knockdown cells, give support to the non-redundancy of YAP/TAZ co-activators in regulating gene expression in the Hippo pathway.
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