Chibby (Cby) is an evolutionarily conserved antagonist of beta-catenin, a 
central player of the canonical Wnt signaling pathway, which acts as a 
transcriptional coactivator. Cby physically interacts with the C-terminal 
activation domain of beta-catenin and blocks its transcriptional activation 
potential through competition with DNA-binding Tcf/Lef transcription factors. 
Our recent study revealed a second mechanism for Cby-mediated beta-catenin 
inhibition in which Cby cooperates with 14-3-3 adaptor proteins to facilitate 
nuclear export of beta-catenin, following phosphorylation of Cby by Akt kinase. 
Therefore, our findings unravel a novel molecular mechanism regulating the 
dynamic nucleo-cytoplasmic trafficking of beta-catenin and provide new insights 
into the cross-talk between the Wnt and Akt signaling pathways. Here, we review 
recent literature concerning Cby function and discuss our current understanding 
of the relationship between Wnt and Akt signaling.