Unknown

Dataset Information

0

Inside-out regulation of E-cadherin conformation and adhesion.


ABSTRACT: Cadherin cell-cell adhesion proteins play key roles in tissue morphogenesis and wound healing. Cadherin ectodomains bind in two conformations, X-dimers and strand-swap dimers, with different adhesive properties. However, the mechanisms by which cells regulate ectodomain conformation are unknown. Cadherin intracellular regions associate with several actin-binding proteins including vinculin, which are believed to tune cell-cell adhesion by remodeling the actin cytoskeleton. Here, we show at the single-molecule level, that vinculin association with the cadherin cytoplasmic region allosterically converts weak X-dimers into strong strand-swap dimers and that this process is mediated by myosin II-dependent changes in cytoskeletal tension. We also show that in epithelial cells, ∼70% of apical cadherins exist as strand-swap dimers while the remaining form X-dimers, providing two cadherin pools with different adhesive properties. Our results demonstrate the inside-out regulation of cadherin conformation and establish a mechanistic role for vinculin in this process.

SUBMITTER: Koirala R 

PROVIDER: S-EPMC8325368 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC3979599 | biostudies-literature
| S-EPMC4571897 | biostudies-literature
| S-EPMC6824599 | biostudies-literature
| S-EPMC4964354 | biostudies-literature
| S-EPMC9055568 | biostudies-literature
| S-EPMC3882713 | biostudies-literature
| S-EPMC2893160 | biostudies-literature
| S-EPMC4395369 | biostudies-literature
| S-EPMC3479437 | biostudies-literature
| S-EPMC3032545 | biostudies-literature