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Review
. 2016 Oct 10;591(1):292-303.
doi: 10.1016/j.gene.2016.07.028. Epub 2016 Jul 14.

An Evolutionary, Structural and Functional Overview of the Mammalian TEAD1 and TEAD2 Transcription Factors

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Free PMC article
Review

An Evolutionary, Structural and Functional Overview of the Mammalian TEAD1 and TEAD2 Transcription Factors

André Landin-Malt et al. Gene. .
Free PMC article

Abstract

TEAD proteins constitute a family of highly conserved transcription factors, characterized by a DNA-binding domain called the TEA domain and a protein-binding domain that permits association with transcriptional co-activators. TEAD proteins are unable to induce transcription on their own. They have to interact with transcriptional cofactors to do so. Once TEADs bind their co-activators, the different complexes formed are known to regulate the expression of genes that are crucial for embryonic development, important for organ formation (heart, muscles), and involved in cell death and proliferation. In the first part of this review we describe what is known of the structure of TEAD proteins. We then focus on two members of the family: TEAD1 and TEAD2. First the different transcriptional cofactors are described. These proteins can be classified in three categories: i), cofactors regulating chromatin conformation, ii), cofactors able to bind DNA, and iii), transcriptional cofactors without DNA binding domain. Finally we discuss the recent findings that identified TEAD1 and 2 and its coactivators involved in cancer progression.

Keywords: Cancer; TEA; TEAD; Transcription factor; VGLL; YAP.

Figures

Figure 1.
Figure 1.
The overall structure of the mammalian TEAD factors is schematized. The domains are defined both by their conservation among the family members and by their amino acid compositions. The numbers represent the amino acid coordinates of each domain in the prototype member TEAD1. The corresponding amino acid coordinates in the TEAD2, TEAD3, and TEAD4 factors are similar.
Figure 2.
Figure 2.
The 3D structure of the TEA domain. A. Hydrophobic surface patch of TEA domain. (B) Superimposition of TEA domain (PDB ID 2HZD) with a structurally homologous protein (MatA1, PDB ID 1AKH, Cyan) bound to DNA (Magenta). TEA: green (Loops) and red (Helices)
Figure 3.
Figure 3.
The 3D structure of YBD from (A) Li et al, 2010. (B) Chen et al, 2010. The YBD was crystallized together with the TEAD binding domain of YAP (Yes/Src associated protein kinase). (C) Tian et al, 2010.

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