Cadherin-bound CTNNB1 (beta-catenin) at the plasma membrane is known to associate with CTNNA1 (alpha-catenin) through the N-terminal domain of beta-catenin (Ozawa and Kemler 1992). CTNNA1 was shown to be a part of the complex of CDH11, CTNND1 and CTNNB1 in the cortex adherens structure formed by the eye lens fiber cells in all three organisms tested: cow, pig and rat (Straub et al. 2003). The co-localization of CTNNA1 with CDH11 at the plasma membrane is dependent on the presence of the C-terminal binding sequence (CBS), involved in CTNNB1 binding (Kiener et al. 2006). While the presence of the juxtamembrane domain (JMD) of CDH11, which binds CTNND1 (p120 catenin, also known as delta-catenin) is not needed for the recruitment of CTNNA1, the JMD of CDH11 was shown to regulate CTNNA1 turnover at adherens junctions. The rate of CTNNA1 turnover is decreased in cells expressing CDH11 that lacks the JMD, leading to formation of a more extensive cortical F actin ring and an increased level of activated RAC1 (Kiener et al. 2006).

Binding of CTNNA1 to cadherin-associated CTNNB1 may be mutually exclusive with binding of vinculin (VCL) (Luegmayr et al. 2000).

Based on studies with other cadherins, CTNNA1 can also be recruited to cadherins through association with JUP (Junctional Plakoglobin, also known as gamma-catenin) (Butz and Kemler 1994; Aberle et al. 1994; Huber et al. 1997), which is known to be an interaction partner of CDH11 (Lee et al. 2018).