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Figure 2


Fig. 2. The structural variety of vertebrate TCF/LEFs. Protein-coding exon structure is shown for a generic invertebrate Tcf gene and generic vertebrate Tcf-1, Lef-1, Tcf-3 and Tcf-4 genes or in HUGO nomenclature, TCF7, LEF1, TCF7L1 and TCF7L2, respectively (from top to bottom, with N-terminal exons on the left and C-terminal exons on the right). Note the four broad domains of TCF proteins: N-terminal domain, central domain, DNA-binding domain and C-terminal tail. Described protein-protein interaction domains and polypeptide motifs that are conserved between invertebrate and vertebrate TCF proteins are indicated between the invertebrate and the vertebrate TCFs. The N-terminal β-catenin-binding domain (BCBD) is marked in green, the interaction domain with the groucho/TLE transcriptional co-repressors in red, the HMG DNA-binding domain in dark blue, the nuclear localisation signal (NLS) in turquoise, the CRARF motif in mid blue and the RKKKCIRY motive in pale blue. Note the central exon coloured yellow, which is an obligatory exon in invertebrate TCFs and in vertebrate TCF-3 and TCF-4, but an alternative exon in vertebrate TCF-1 and LEF-1. Described protein-protein interaction domains and polypeptide motives in certain Tcf genes that are conserved among vertebrates but apparently not with invertebrate Tcf genes are indicated below the vertebrate TCFs. They are the LVPQ and SxxSS motives in the central domain and the C-terminal domain described as a CtBP-binding domain (purple) present in alternatively spliced vertebrate TCF-4 isoforms, but always present in vertebrate TCF-3. The identified SUMOylation sites in LEF-1 (K25) and in TCF-4 (K297) are indicated in grey. Alternative translation initiation sites for TCF-1 and LEF-1 are indicated, which produce {Delta}N-TCF isoforms lacking the β-catenin-binding domain (BCBD). For further detail, see main text and recent molecular review (Arce et al., 2006).





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