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Structural insights into the YAP and TEAD complex.

Li Z, Zhao B, Wang P, Chen F, Dong Z, Yang H, Guan KL, Xu Y
Genes Dev 24 235-40 (2010)
Cited: 212 times
EuropePMC logo PMID: 20123905

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.

Reviews - 3kys mentioned but not cited (7)

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Articles - 3kys mentioned but not cited (32)

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Reviews citing this publication (52)

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