Structure of the Dimerization and β-Catenin- Binding Region of α-Catenin

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α-Catenin Is a Molecular Switch that Binds E-Cadherin-β-Catenin and Regulates Actin-Filament Assembly (2005, unknown): “The crystal structure of the N-terminal domain of α-catenin revealed that the dimerization domain overlaps the β-catenin binding domain (Pokutta and Weis, 2000).”
Adherens junctions: from molecules to morphogenesis (2010, background): “However, αE-catenin (the mammalian α-catenin isoform with which these experiments were carried out) binds to actin preferentially as a dimer, and the dimerization domain in αE-catenin overlaps with its β-catenin-binding sit”
The many faces and functions of β‐catenin (2012, unknown): “Binding of a-catenin stabilizes b-catenin in the hinged form, and E-cadherin can bind simultaneously (Pokutta and Weis, 2000; Huber and Weis, 2001).”
Deconstructing the cadherin-catenin-actin complex. (2005, background): “The cadherin cytoplasmic domain forms a high affinity , 1:1 complex with b-catenin, and b-catenin binds with lower affinity to a-catenin (Aberle et al., 1994; Hinck et al., 1994; Pokutta and Weis, 2000; Huber and Weis, 2001).”