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Structural insights into the YAP and TEAD complex.


ABSTRACT: The Yes-associated protein (YAP) transcriptional coactivator is a key regulator of organ size and a candidate human oncogene inhibited by the Hippo tumor suppressor pathway. The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression. Here we report the three-dimensional structure of the YAP (residues 50-171)-TEAD1 (residues 194-411) complex, in which YAP wraps around the globular structure of TEAD1 and forms extensive interactions via three highly conserved interfaces. Interface 3, including YAP residues 86-100, is most critical for complex formation. Our study reveals the biochemical nature of the YAP-TEAD interaction, and provides a basis for pharmacological intervention of YAP-TEAD hyperactivation in human diseases.

SUBMITTER: Li Z 

PROVIDER: S-EPMC2811825 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature

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Structural insights into the YAP and TEAD complex.

Li Ze Z   Zhao Bin B   Wang Ping P   Chen Fei F   Dong Zhenghong Z   Yang Huirong H   Guan Kun-Liang KL   Xu Yanhui Y  

Genes & development 20100201 3


The Yes-associated protein (YAP) transcriptional coactivator is a key regulator of organ size and a candidate human oncogene inhibited by the Hippo tumor suppressor pathway. The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression. Here we report the three-dimensional structure of the YAP (residues 50-171)-TEAD1 (residues 194-411) complex, in which YAP wraps around the globular structure of TEAD1 and forms extensive interactions via three highly conserv  ...[more]

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