PMID- 20123908
OWN - NLM
STAT- MEDLINE
DCOM- 20100301
LR  - 20211203
IS  - 1549-5477 (Electronic)
IS  - 0890-9369 (Print)
IS  - 0890-9369 (Linking)
VI  - 24
IP  - 3
DP  - 2010 Feb 1
TI  - Structural basis of YAP recognition by TEAD4 in the hippo pathway.
PG  - 290-300
LID - 10.1101/gad.1865310 [doi]
AB  - The Hippo signaling pathway controls cell growth, proliferation, and apoptosis by 
      regulating the expression of target genes that execute these processes. Acting 
      downstream from this pathway is the YAP transcriptional coactivator, whose 
      biological function is mediated by the conserved TEAD family transcription 
      factors. The interaction of YAP with TEADs is critical to regulate Hippo 
      pathway-responsive genes. Here, we describe the crystal structure of the 
      YAP-interacting C-terminal domain of TEAD4 in complex with the TEAD-interacting 
      N-terminal domain of YAP. The structure reveals that the N-terminal region of YAP 
      is folded into two short helices with an extended loop containing the PXXPhiP 
      motif in between, while the C-terminal domain of TEAD4 has an immunoglobulin-like 
      fold. YAP interacts with TEAD4 mainly through the two short helices. Point 
      mutations of TEAD4 indicate that the residues important for YAP interaction are 
      required for its transforming activity. Mutagenesis reveals that the PXXPhiP 
      motif of YAP, although making few contacts with TEAD4, is important for TEAD4 
      interaction as well as for the transforming activity.
FAU - Chen, Liming
AU  - Chen L
AD  - The Cancer and Developmental Cell Biology Division, Institute of Molecular and 
      Cell Biology, Proteos, Singapore.
FAU - Chan, Siew Wee
AU  - Chan SW
FAU - Zhang, XiaoQian
AU  - Zhang X
FAU - Walsh, Martin
AU  - Walsh M
FAU - Lim, Chun Jye
AU  - Lim CJ
FAU - Hong, Wanjin
AU  - Hong W
FAU - Song, Haiwei
AU  - Song H
LA  - eng
SI  - PDB/3JUA
PT  - Journal Article
PL  - United States
TA  - Genes Dev
JT  - Genes & development
JID - 8711660
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (TEA Domain Transcription Factors)
RN  - 0 (TEAD4 protein, human)
RN  - 0 (Tead4 protein, mouse)
RN  - 0 (Transcription Factors)
RN  - 0 (YAP-Signaling Proteins)
RN  - 0 (YY1AP1 protein, human)
RN  - 0 (Yap1 protein, mouse)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing/*chemistry/genetics/metabolism
MH  - Animals
MH  - Cell Cycle Proteins
MH  - Crystallography, X-Ray
MH  - DNA-Binding Proteins/*chemistry/genetics/metabolism
MH  - Humans
MH  - Mice
MH  - Models, Molecular
MH  - Muscle Proteins/*chemistry/metabolism
MH  - Nuclear Proteins/chemistry/metabolism
MH  - Phosphoproteins/*chemistry/metabolism
MH  - Protein Isoforms/chemistry/metabolism
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Protein Structure, Tertiary
MH  - *Signal Transduction
MH  - TEA Domain Transcription Factors
MH  - Transcription Factors/*chemistry/metabolism
MH  - Transcriptional Activation
MH  - YAP-Signaling Proteins
PMC - PMC2811830
EDAT- 2010/02/04 06:00
MHDA- 2010/03/02 06:00
PMCR- 2010/08/01
CRDT- 2010/02/04 06:00
PHST- 2010/02/04 06:00 [entrez]
PHST- 2010/02/04 06:00 [pubmed]
PHST- 2010/03/02 06:00 [medline]
PHST- 2010/08/01 00:00 [pmc-release]
AID - 24/3/290 [pii]
AID - 10.1101/gad.1865310 [doi]
PST - ppublish
SO  - Genes Dev. 2010 Feb 1;24(3):290-300. doi: 10.1101/gad.1865310.