CHD8 is a ATP-dependent chromatin remodeling factor that binds directly to beta-catenin to repress transcription of WNT target genes (Thompson et al, 2008; Sakamoto et al, 2000). ChIP studies show that CHD8 is recruited to the promoters of several beta-catenin-responsive targets, and knockdown of CHD8 results in induction of these target genes in vivo (Thompson et al, 2008). An N-terminal fragment of CHD was independently identified as the rat protein Duplin. Duplin was shown to negatively regulate WNT target gene expression by competing with TCF7L2 for beta-catenin binding (Sakamoto et al, 2000; Kobayashi et al, 2002). A corresponding fragment of CHD8 has not been identified in human cells and its significance is not clear.