journal article Open Access Nov 20, 2020

Study of the TEAD‐binding domain of the YAP protein from animal species

Protein Science Vol. 30 No. 2 pp. 339-349 · Wiley
Abstract
AbstractThe Hippo signaling pathway, which plays a central role in the control of organ size in animals, is well conserved in metazoans. The most downstream elements of this pathway are the TEAD transcription factors that are regulated by their association with the transcriptional coactivator YAP. Therefore, the creation of the binding interface that ensures the formation of the YAP:TEAD complex is a critical molecular recognition event essential for the development/survival of many living organisms. In this report, using the available structural information on the YAP:TEAD complex, we study the TEAD‐binding domain of YAP from different animal species. This analysis of more than 400 amino acid sequences reveals that the residues from YAP involved in the formation of the two main contact regions with TEAD are very well conserved. Therefore, the binding interface between YAP and TEAD, as found in humans, probably appeared at an early evolutionary stage in metazoans. We find that, in contrast to most other animal species, several Actinopterygii species possess YAP variants with a different TEAD‐binding domain. However, these variants bind to TEAD with a similar affinity. Our studies show that the protein identified as a YAP homolog in Caenorhabditis elegans does not contain the TEAD‐binding domain found in YAP of other metazoans. Finally, we do not identify in non‐metazoan species, amino acid sequences containing both a TEAD‐binding domain, as in metazoan YAP, and WW domain(s).
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References
47
[3]
The Hippo pathway in the heart: pivotal roles in development, disease, and regeneration

Jun Wang, Shijie Liu, Todd Heallen et al.

Nature Reviews Cardiology 10.1038/s41569-018-0063-3
[10]
YAP/TAZ at the Roots of Cancer

Francesca Zanconato, Michelangelo Cordenonsi, Stefano Piccolo

Cancer Cell 10.1016/j.ccell.2016.05.005
[11]
Gibault F "Toward the discovery of a novel class of YAP‐TEAD interaction inhibitors by virtual screening approach targeting the YAP‐TEAD protein‐protein interface" Cancer (2018) 10.3390/cancers10050140
[12]
Targeting the Hippo Pathway and Cancer through the TEAD Family of Transcription Factors

Jeffrey Holden, Christian Cunningham

Cancers 10.3390/cancers10030081
[21]
Structural insights into the YAP and TEAD complex

Ze Li, Bin Zhao, Ping Wang et al.

Genes & Development 10.1101/gad.1865810
[24]
Structure-Based Design and Synthesis of Potent Cyclic Peptides Inhibiting the YAP–TEAD Protein–Protein Interaction

Zhisen Zhang, Zhaohu Lin, Zheng Zhou et al.

ACS Medicinal Chemistry Letters 10.1021/ml500160m
[27]
WebLogo: A Sequence Logo Generator: Figure 1

Gavin E. Crooks, Gary Hon, John-Marc Chandonia et al.

Genome Research 10.1101/gr.849004
[33]
An analysis of protein domain linkers: their classification and role in protein folding

Richard A. George, Jaap Heringa

Protein Engineering, Design and Selection 10.1093/protein/15.11.871
[34]
Effect of Proline and Glycine Residues on Dynamics and Barriers of Loop Formation in Polypeptide Chains

Florian Krieger, Andreas Möglich, Thomas Kiefhaber

Journal of the American Chemical Society 10.1021/ja042798i
[35]
The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery

Elena Papaleo, Giorgio Saladino, Matteo Lambrughi et al.

Chemical Reviews 10.1021/acs.chemrev.5b00623
[39]
Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

PuiYee Chan, Xiao Han, Baohui Zheng et al.

Nature Methods 10.1038/nchembio.2036
[44]
Structural Basis of Amino Acid α Helix Propensity

Michael Blaber, Xue-jun Zhang, Brian W. Matthews

Science 10.1126/science.8503008
[46]
Ensembl Genomes 2020—enabling non-vertebrate genomic research

Kevin L Howe, Bruno Contreras-Moreira, Nishadi De Silva et al.

Nucleic Acids Research 10.1093/nar/gkz890
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