Interaction of cadherin with Beta/gamma catenin, alpha catenin and p120 catenin

Stable Identifier
Reaction [binding]
Homo sapiens
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The cytoplasmic tails of classical cadherins form a multiprotein complex with alpha-catenin, beta/gamma-catenins and p120 catenin (p120ctn) (Gumbiner, 2005). Beta-catenin and p120ctn directly interact with the cadherin molecule through highly conserved regions in the membrane-distal and membrane-proximal domains, respectively, of the cadherin. The interactions with beta-catenin and p120ctn regulate cadherin localization at cell-cell contacts as well as its adhesive activity (Halbleib and Nelson, 2006). The association of beta-catenin and alpha-catenin probably serves to link the cadherin-catenin complex to the F-actin cytoskeleton through the protein ELPIN (Abe and Takeichi, 2008). Independently of its association with the cadherin-catenin complex, alpha-catenin also regulates the bundling and growth of actin filaments at sites of cell-cell contact formation (Drees et al., 2005; Weis and Nelson, 2006).

Literature References
PubMed ID Title Journal Year
7806582 E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton

Hülsken, J, Birchmeier, W, Behrens, J

J Cell Biol 1994
Participant Of
Orthologous Events