Proteins of the dishevelled family (Dsh and Dvl) play a key role in the transduction of the Wg/Wnt signal (see <PDOC00219>) from the cell surface to the nucleus: in response to Wnt signal, they block the degradation of β-catenin by interacting with the scaffolding protein axin. The N-terminus of proteins of the dishevelled family and the C-terminus of proteins of the axin family share a region of homology of about 85 amino acids, which has been called DIX for DIshevelled and aXin [1]. The DIX domain is found associated with PDZ (see <PDOC50106>) and DEP (see <PDOC50186>) domains in proteins of the dishevelled family and with an RGS domain (see <PDOC50132>) in proteins of the axin family. DIX has been shown to be a protein-protein interaction domain that is important for homo- and hetero-oligomerization of proteins of the dishevelled and axin families [2,3,4,5]. The DIX domain has also be shown to be a signalling module that can target proteins to actin stress fibres and cytoplasmic vesicles to control Wnt signalling [6,7].

The Dvl2 DIX domain has been shown to form a predominantly helical structure [6].

The profile we developed covers the entire DIX domain.