LAR, PTPR-mu, Actin, E-cadherin, AF-6, Beta-catenin, p120- catenin, Fyn, M-cadherin, P-cadherin, N-cadherin, VE-cadherin, N-cadherin, Cortactin, N-WASP, Arp2/3, Actin cytoskeletal, Plakoglobin, VE-cadherin, E-cadherin, Fer, FAK1, c-Src, DEP-1, Met, P-cadherin, CDC42, Alpha-catenin, SHP-2, Formin
Cadherin-mediated cell adhesion
Cadherins are calcium-dependent homophilic cell adhesion proteins essential for tissue organization. Establishment of stable cell-cell adhesion depends on association of classical Cadherins with Catenins, which links cell surface adhesion and recognition to both Actin cytoskeleton and cell signaling pathways. Catenin (cadherin-associated protein), beta 1 (Beta-catenin) binds with high affinity to the distal Cadherin cytoplasmic tail and, in turn, recruits Catenin (cadherin-associated protein), alpha 1, 102kDa ( Alpha-catenin ) to the complex. Alpha-catenin binds to Actin filaments directly and can also associate with a range of other actin-binding proteins such as Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 4 ( AF-6 ) and Formin. In contrast, Catenin delta 1 ( p120-catenin ) binds directly to Cadherin independently of the other catenins. Cadherin-Catenins complex can further interact with a range of signaling molecules which participate in either cellular signaling or control of cytoskeletal dynamics . Stability of the Cadherin/ Catenins complex and thereby the integrity of adherent junction is controlled by phosphorylation/ dephosphorylation. Phosphorylation of Beta-catenin by receptor- and non-receptor-types tyrosine kinases results in dissociation of Alpha-catenin from Beta-catenin with concomitant loss of cadherin adhesion, whereas tyrosine phosphatases ensure or restore the integrity of Cadherin -mediated adhesions .