ABSTRACT
Dishevelled proteins are multifunctional and highly conserved. These proteins are also required for the specification of cell fate and polarity by secreted Wnt proteins. To investigate the molecular mechanism of Dishevelled in mediating Wnt signal transduction, a mouse 11.5dpc embryo library was screened by yeast-two-hybrid system to find mouse Dishevelled2 DEP domain and C-terminal interacting proteins. 15 possitive clones were identified from 4.1 x 10(6) transformants. The DNA sequences of the positive AD/library plasmids were determined. The BLAST results revealed that one of the positive clones contained N-terminus cDNA fragments (amino acids 6-122) of Gli3 protein. The interaction between Dv12 and Gli3 detected by yeast two-hybrid system suggests that Gli3 might play a role in some biological processes with Dishevelled.