Catenins are proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified became known as alpha-catenin and beta-catenin. Alpha-catenin can bind to beta-catenin and can also bind actin. Beta-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as gamma-catenin and delta-catenin have been identified. The name "catenin" was originally selected ('catena' means 'chain' in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton.
Catenins and cadherin function
F9 embryonal carcinoma cells are similar to the P19 cells shown in Figure 1 and normally have cell-to-cell adhesion mediated by E-cadherin with beta-catenin bound to the cytoplasmic domain of E-cadherin. F9 cells were genetically engineered to lack beta-catenin, resulting in increased association of plakoglobin with E-cadherin . In F9 cells lacking both beta-catenin and plakoglobin, very little E-cadherin and alpha-catenin accumulated at the cell surface . Mice lacking beta-catenin have defective embyos. Mice engineered to specifically have vascular endothelium cells deficient in beta-catenin showed disrupted adhesion between vascular endothelial cells . Mice lacking plakoglobin have cell adhesion defects in many tissues, although beta-catenin substitutes for plakoglobin at many cellular junctions . Keratinocytes engineered to not express alpha-catenin have disrupted cell adhesion . A tumor cell line with defective delta-catenin, low levels of E-cadherin and poor cell-to-cell adhesion could be reverted to normal epithelial morphology and increased E-cadherin levels by expression of normal levels of functional delta-catenin .
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