In the absence of a WNT signal, promoter-bound TCF/LEF is bound by one of four Groucho homologues, TLE1, 2, 3 or 4 (Levanon et al, 1998; Brantjes et al, 2001; Daniels and Weis, 2005). Groucho/TLE proteins are co-repressors for a variety of DNA-binding transcription factors and mediate repression at least in part through their interaction with histone deacetylases such as RPD3/HDAC1 (Arce et al, 2009; Brantjes et al, 2001; Chen et al, 1999; reviewed in Chen and Courey, 2000). Groucho proteins have been shown to homo-tetramerize through a glutamine rich Q domain at the N-terminus, and this oligomerization is required for repression. The Q domain is also sufficient for interaction with TCF/LEF proteins (Brantjes et al, 2001; Chen et al, 1998; Pinto and Lobe, 1996; Song et al, 2004). Studies with purified proteins have shown that human TLE1 and 2 bind to an amino-terminal truncated form of LEF1(69-397) with an affinity comparable to that for full length LEF1 (Daniels and Weis, 2005)
Arce, L, Waterman, ML, Pate, KT
Hasson, P, Paroush, Z, Song, H, Courey, AJ
Weis, WI, Daniels, DL
van De Wetering, M, Clevers, HC, Brantjes, H, Roose, J
Paroush, Z, Goldstein, RE, Groner, Y, Tang, H, Bernstein, Y, Levanon, D, Goldenberg, D, Stifani, S
Chen, G, Courey, AJ, Nguyen, PH
Chen, G, Mische, S, Fernandez, J, Courey, AJ
Pinto, M, Lobe, CG
Chen, G, Courey, AJ
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