An ensemble of flexible conformations underlies mechanotransduction by the cadherin-catenin adhesion complex.

ABSTRACT: The cadherin-catenin adhesion complex is the central component of the cell-cell adhesion adherens junctions that transmit mechanical stress from cell to cell. We have determined the nanoscale structure of the adherens junction complex formed by the ?-catenin•?-catenin•epithelial cadherin cytoplasmic domain (ABE) using negative stain electron microscopy, small-angle X-ray scattering, and selective deuteration/small-angle neutron scattering. The ABE complex is highly pliable and displays a wide spectrum of flexible structures that are facilitated by protein-domain motions in ?- and ?-catenin. Moreover, the 107-residue intrinsically disordered N-terminal segment of ?-catenin forms a flexible "tongue" that is inserted into ?-catenin and participates in the assembly of the ABE complex. The unanticipated ensemble of flexible conformations of the ABE complex suggests a dynamic mechanism for sensitivity and reversibility when transducing mechanical signals, in addition to the catch/slip bond behavior displayed by the ABE complex under mechanical tension. Our results provide mechanistic insight into the structural dynamics for the cadherin-catenin adhesion complex in mechanotransduction.

SUBMITTER: Bush M 

PROVIDER: S-EPMC6815173 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature