E-cadherin phosphorylation occurs during its biosynthesis to promote its cell surface stability and adhesion.

ABSTRACT: E-cadherin is highly phosphorylated within its β-catenin-binding region, and this phosphorylation increases its affinity for β-catenin in vitro. However, the identification of key serines responsible for most cadherin phosphorylation and the adhesive consequences of modification at such serines have remained unknown. In this study, we show that as few as three serines in the β-catenin-binding domain of E-cadherin are responsible for most radioactive phosphate incorporation. These serines are required for binding to β-catenin and the mutual stability of both E-cadherin and β-catenin. Cells expressing a phosphodeficient (3S>A) E-cadherin exhibit minimal cell-cell adhesion due to enhanced endocytosis and degradation through a lysosomal compartment. Conversely, negative charge substitution at

SUBMITTER: McEwen AE 

PROVIDER: S-EPMC4142610 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature