The spatial and functional organization of cells in tissues is determined by cell-cell adhesion, which is initiated through interactions between the extracellular domains of cadherin proteins and strengthened by linkage to the actin cytoskeleton. The prevailing view is that this linkage occurs through β-catenin and α-catenin, but the quaternary complex has never been demonstrated. This study tests this hypothesis and finds that α-catenin does not simultaneously interact with actin filaments and the E-cadherin-β-catenin complex, even in the presence of actin-binding proteins like vinculin and α-actinin. Direct analysis in polarized cells shows that the mobilities of E-cadherin, β-catenin, and α-catenin are similar regardless of actin assembly dynamics, while actin and actin-binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously thought. The study also examines the dynamics of these proteins at mature cell-cell contacts, finding that membrane-associated actin is highly dynamic and rapidly exchanges with a cytoplasmic actin pool. Actin binding proteins, such as vinculin and α-actinin, do not show α-catenin-like turnover and do not mediate a stable linkage between the cadherin-catenin complex and actin filaments. Overall, the findings challenge the assumption of a static linkage between the cadherin-catenin complex and the actin cytoskeleton, suggesting that adhesion must be a dynamic process to enable morphogenetic changes during cell and tissue development.The spatial and functional organization of cells in tissues is determined by cell-cell adhesion, which is initiated through interactions between the extracellular domains of cadherin proteins and strengthened by linkage to the actin cytoskeleton. The prevailing view is that this linkage occurs through β-catenin and α-catenin, but the quaternary complex has never been demonstrated. This study tests this hypothesis and finds that α-catenin does not simultaneously interact with actin filaments and the E-cadherin-β-catenin complex, even in the presence of actin-binding proteins like vinculin and α-actinin. Direct analysis in polarized cells shows that the mobilities of E-cadherin, β-catenin, and α-catenin are similar regardless of actin assembly dynamics, while actin and actin-binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously thought. The study also examines the dynamics of these proteins at mature cell-cell contacts, finding that membrane-associated actin is highly dynamic and rapidly exchanges with a cytoplasmic actin pool. Actin binding proteins, such as vinculin and α-actinin, do not show α-catenin-like turnover and do not mediate a stable linkage between the cadherin-catenin complex and actin filaments. Overall, the findings challenge the assumption of a static linkage between the cadherin-catenin complex and the actin cytoskeleton, suggesting that adhesion must be a dynamic process to enable morphogenetic changes during cell and tissue development.