α-catenin middle- and actin-binding domain unfolding mutants differentially impact epithelial strength and sheet migration.

ABSTRACT: α-catenin (α-cat) displays force-dependent unfolding and binding to actin filaments through direct and indirect means, but features of adherens junction structure and function most vulnerable to loss of these allosteric mechanisms have not been directly compared. By reconstituting an α-cat F-actin-binding domain unfolding mutant known to exhibit enhanced binding to actin (α-cat-H0-FABD⁺) into α-cat knockout Madin Darby Canine Kidney (MDCK) cells, we show that partial loss of the α-cat catch bond mechanism (via an altered H0 α-helix) leads to stronger epithelial sheet integrity with greater colocalization between the α-cat-H0-FABD⁺ mutant and actin. α-cat-H0-FABD⁺ -expressing cells are less efficient at closing scratch-wounds, suggesting reduced capacity for

SUBMITTER: Quinn JM 

PROVIDER: S-EPMC11151094 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature