Disease relevance of pygo

• Humans possess two Pygo proteins, both of which are required for TCF-mediated transcription in colorectal cancer cells [1].

High impact information on pygo

• Pygopus and Legless target Armadillo/beta-catenin to the nucleus to enable its transcriptional co-activator function [2].
• Here, we show that the nuclear localization of Lgs entirely depends on Pygo, which itself is constitutively localized to the nucleus; thus, Pygo functions as a nuclear anchor [2].
• We show that Wg signaling is diminished during embryogenesis and imaginal disc development in the absence of pygo activity [3].
• We further show that Pygo can form a complex with Arm in vivo and possesses a transcription activation domain(s) [3].
• The pygopus mutant phenotype is highly, though not exclusively, specific for Wg signaling [4].

Biological context of pygo

• Epistasis experiments indicate that Pygopus acts downstream of Armadillo nuclear import, consistent with the nuclear location of heterologously expressed protein [4].
• Pygopus contains a PHD finger at its C terminus, a motif often found in chromatin remodeling factors [4].

Anatomical context of pygo

• Here, we report that Pygo is associated constitutively with dTCF target genes in Drosophila salivary glands and tissue-culture cells [5].
• Here, we analyse the mode of action of Pan, Arm, Lgs, and Pygo in Drosophila cultured cells [6].

Associations of pygo with chemical compounds

• Wingless-Independent Association of Pygopus with dTCF Target Genes [5].
• We provide evidence that together these four proteins form a 'chain of adaptors' linking the NH2-terminal homology domain (NHD) of Pygo to the DNA-binding domain of Pan. We show that the NHD has potent transcriptional activation capacity, which differs from that of acidic activator domains and depends on a conserved NPF tripeptide [6].

References