TY - JOUR TI - Dissection of the interaction between the intrinsically disordered YAP protein and the transcription factor TEAD AU - Mesrouze, Yannick AU - Bokhovchuk, Fedir AU - Meyerhofer, Marco AU - Fontana, Patrizia AU - Zimmermann, Catherine AU - Martin, Typhaine AU - Delaunay, Clara AU - Erdmann, Dirk AU - Schmelzle, Tobias AU - Chène, Patrick A2 - Clarke, Jane VL - 6 PY - 2017 DA - 2017/04/21 SP - e25068 C1 - eLife 2017;6:e25068 DO - 10.7554/eLife.25068 UR - https://doi.org/10.7554/eLife.25068 AB - TEAD (TEA/ATTS domain) transcription factors are the most distal effectors of the Hippo pathway. YAP (Yes-associated protein) is a coactivator protein which, upon binding to TEAD proteins, stimulates their transcriptional activity. Since the Hippo pathway is deregulated in various cancers, designing inhibitors of the YAP:TEAD interaction is an attractive therapeutic strategy for oncology. Understanding the molecular events that take place at the YAP:TEAD interface is therefore important not only to devise drug discovery approaches, but also to gain knowledge on TEAD regulation. In this report, combining single site-directed mutagenesis and double mutant analyses, we conduct a detailed analysis on the role of several residues located at the YAP:TEAD interface. Our results provide quantitative understanding of the interactions taking place at the YAP:TEAD interface and give insights into the formation of the YAP:TEAD complex and more particularly on the interaction between TEAD and the Ω-loop found in YAP. KW - protein-protein interaction KW - intrinsically disordered protein KW - molecular recognitiom JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -