Xenbase Image ID: 130490

Figure 8. xYAP deletion mutants exhibit differential activities.(A) Cartoons of the xYAP mutants created to determine which protein-protein interaction domain(s) is important for the in vivo gain-of-function phenotypes described in Figures 4–6. Deletions or mutations are indicated by color loss: the TEAD-binding site (xYAPΔTBS, purple), the LATS phosphorylation site (cActive xYAP, orange), the two WW domains (xYAPΔWW, red), the N-terminus (xYAP, ΔN-term) containing both the hnRNP U and TEAD-binding sites, and the PDZ-binding motif (xYAPΔC-term, fuchsia) at the C-terminus. (B) The percentage of embryos showing expansion of sox2-expressing neural plate cells or expansion of pax3-expressing neural crest progenitor (NCP) cells after injection of each of the mutant forms of xYAP. Note that cActive xYAP, which prevents YAP from leaving the nucleus, is as effective as wild type YAP. However, all other mutant forms reduce this phenotype. Sample sizes are presented in Table 1. (C) The percentage of embryos showing reduced gene expression after injection of each mutant form of xYAP. Deletion of the WW domains or of the PDZ-binding motif interfered the most with repression of pax3+ hatching gland (HG) progenitors. Loss of neural plate differentiation (p27xic1) and a PPE marker (sox11) were maintained at high frequencies with each xYAP mutant, indicating that interactions at one or more of the remaining domains are sufficient to downregulate these genes. However, xYAP-mediated loss of somitic muscle (myoD) and epidermal (cyto-keratin) differentiation was specifically reduced by deletion of its PDZ-binding motif. Image published in: Gee ST et al. (2011) Image downloaded from an Open Access article in PubMed Central. This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. Larger Image Printer Friendly View

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