Homologous Superfamily

DIX domain superfamily (IPR038207)

Short name: DIX_dom_sf

Overlapping entries


Proteins of the dishevelled family (Dsh and Dvl) play a key role in the transduction of the Wg/Wnt signal from the cell surface to the nucleus: in response to Wnt signal, they block the degradation of beta- 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 [PMID: 9407023]. The DIX domain is found associated with PDZ and DEP domains in proteins of the dishevelled family and with an RGS domain 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 [PMID: 10330181, PMID: 10318824, PMID: 11041490, PMID: 11027605]. 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 [PMID: 12384700].

The Dvl2 DIX domain has been shown to form a predominantly helical structure [PMID: 12384700].

A third type of DIX domain-possessing protein, known as Coiled-coil-DIX1 (Ccd1) or Dixin, forms homomeric and heteromeric complexes with Dvl and Axin and is positive regulator of Wnt signaling [PMID: 15857680].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.