Epidermal growth factor receptor is an essential component in E-cadherin force transduction complexes.

ABSTRACT: We present evidence that the association of the epithelial (E)-cadherin (CHD1) extracellular domain and epidermal growth factor receptor (EGFR, ErbB1) is obligatory for cadherin force transduction signaling. E-cadherin and EGFR associate at cell surfaces, independent of their cytoplasmic domains, and tension on E-cadherin activates EGFR signaling. Using engineered E-cadherin mutants that disrupt co-immunoprecipitation with EGFR, but not adhesion, we show that the hetero-receptor complex is required to mechanically activate signaling and downstream cytoskeletal remodeling at cadherin adhesions. The mutants localized the essential region on E-cadherin to domain 4 of the extracellular region (EC4). The ectodomain is also required for hetero-receptor colocalization at intercellular junctions.

SUBMITTER: Zou Y 

PROVIDER: S-EPMC12669962 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature