High impact information on ctnnb1

• Analysis of the mutant phenotype shows that at least two regions of the N-cadherin cytoplasmic domain can inhibit adhesion and that the mutant cadherin can inhibit catenin binding to E-cadherin [1].
• In immunofluorescence tests, alpha catenin is colocalized with cadherins at the plasma membrane [2].
• Isolation and characterization of XKaiso, a transcriptional repressor that associates with the catenin Xp120(ctn) in Xenopus laevis [3].
• The catenin p120(ctn) (formerly p120cas) was first identified as a src- and receptor-protein tyrosine kinase substrate and later shown to interact directly with cadherins [4].
• Phosphorylation is not likely to be the cause of cadherin and catenin disappearance from the tissues of strongly aberrant frog embryos [5].

Analytical, diagnostic and therapeutic context of ctnnb1

• Immunofluorescence and immuno-electron microscopy have been applied to elucidate the nature and localization of cadherin/catenin-mediated cell-cell adhesion sites in adult muscle tissues [6].

References