There are four dynamically and functionally distinct populations of E-cadherin in cell junctions

Biology Open

Kurt I. Anderson¹  Zahra Erami¹  Paul Timpson¹  Wu Yao²  Ronen Zaidel-Bar² 

[1] Cancer Research UK Beatson Institute, Glasgow G11 7DU, UK;Mechanobiology Institute, National University of Singapore, Singapore 117411;

关键词: E-cadherin;    FRAP;    Cell adhesion;    Super-resolution microscopy;   

DOI  :  10.1242/bio.014159

来源: DOAJ

【 摘 要 】

E-cadherin is a trans-membrane tumor suppressor responsible for epithelial cell adhesion. E-cadherin forms adhesive clusters through combined extra-cellular cis- and trans-interactions and intracellular interaction with the actin cytoskeleton. Here we identify four populations of E-cadherin within cell junctions based on the molecular interactions which determine their mobility and adhesive properties. Adhesive and non-adhesive populations of E-cadherin each consist of mobile and immobile fractions. Up to half of the E-cadherin immobilized in cell junctions is non-adhesive. Incorporation of E-cadherin into functional adhesions require all three adhesive interactions, with deletion of any one resulting in loss of effective cell-cell adhesion. Interestingly, the only interaction which could independently slow the diffusion of E-cadherin was the tail-mediated intra-cellular interaction. The adhesive and non-adhesive mobile fractions of E-cadherin can be distinguished by their sensitivity to chemical cross-linking with adhesive clusters. Our data define the size, mobility, and adhesive properties of four distinct populations of E-cadherin within cell junctions, and support association with the actin cytoskeleton as the first step in adhesion formation.

【 授权许可】

Unknown