Format

Send to:

Choose Destination
See comment in PubMed Commons below
Genes Dev. 2010 Feb 1;24(3):235-40. doi: 10.1101/gad.1865810.

Structural insights into the YAP and TEAD complex.

Author information

  • 1School of Life Sciences, Fudan University, Shanghai 200433, China.

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.

PMID:
20123905
[PubMed - indexed for MEDLINE]
PMCID:
PMC2811825
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk