Directed actin polymerization is the driving force for epithelial cell- cell adhesion

865Citations
Citations of this article
425Readers
Mendeley users who have this article in their library.

Abstract

We have found that epithelial cells engage in a process of cadherin- mediated intercellular adhesion that utilizes calcium and actin polymerization in unexpected ways. Calcium stimulates filopodia, which penetrate and embed into neighboring cells. E-cadherin complexes cluster at filopodia tips, generating a two-rowed zipper of embedded puncta. Opposing cell surfaces are clamped by desmosomes, while vinculin, zyxin, VASP, and Mena are recruited to adhesion zippers by a mechanism that requires α- catenin. Actin reorganizes and polymerizes to merge puncta into a single row and seal cell borders. In keratinocytes either null for α-catenin or blocked in VASP/Mena function, filopodia embed, but actin reorganization/polymerization is prevented, and membranes cannot seal. Taken together, a dynamic mechanism for intercellular adhesion is unveiled involving calcium-activated filopodia penetration and VASP/Mena-dependent actin reorganization/polymerization.

Cite

CITATION STYLE

APA

Vasioukhin, V., Bauer, C., Yin, M., & Fuchs, E. (2000). Directed actin polymerization is the driving force for epithelial cell- cell adhesion. Cell, 100(2), 209–219. https://doi.org/10.1016/S0092-8674(00)81559-7

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free