Mechanism of the cadherin-catenin F-actin catch bond interaction

• DOI: 10.1101/2022.05.06.490842
• Publication Date: 2022-05-09T11:55:11Z
• Authors: Amy Wang; Alexander R. Dunn; William I. Weis
• Keywords: Ternary complex; Adherens junction

Abstract Mechanotransduction at cell-cell adhesions is crucial for the structural integrity, organization, and morphogenesis of epithelia. At junctions, ternary E-cadherin/β-catenin/αE-catenin complexes sense transmit mechanical load by binding to F-actin. The interaction with F-actin, described as a two-state catch bond, weak in solution but strengthened applied force due force-dependent transitions between strong actin-binding states. Here, we provide direct evidence from optical trapping experiments that bond property principally resides αE-catenin domain (ABD). Consistent our previously proposed model, deletion first helix five-helix ABD bundle enables stable interactions F-actin under minimal are well-described single-state slip even when complexed β-catenin E-cadherin. Our data argue conserved mechanism adhesion proteins structurally similar ABDs. We also demonstrate stably bound strengthens load-dependent neighboring complex presence other domains weakens this effect. These results mechanistic insight cooperative cadherin-catenin which regulate dynamic cytoskeletal linkages epithelial tissues.