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• W4210368427 abstract "Increased intercellular tension is associated with enhanced cell proliferation and tissue growth. Here, we present evidence for a force-transduction mechanism that links mechanical perturbations of epithelial (E)-cadherin (CDH1) receptors to the force-dependent activation of epidermal growth factor receptor (EGFR, ERBB1)-a key regulator of cell proliferation. Here, coimmunoprecipitation studies first show that E-cadherin and EGFR form complexes at the plasma membrane that are disrupted by either epidermal growth factor (EGF) or increased tension on homophilic E-cadherin bonds. Although force on E-cadherin bonds disrupts the complex in the absence of EGF, soluble EGF is required to mechanically activate EGFR at cadherin adhesions. Fully quantified spectral imaging fluorescence resonance energy transfer further revealed that E-cadherin and EGFR directly associate to form a heterotrimeric complex of two cadherins and one EGFR protein. Together, these results support a model in which the tugging forces on homophilic E-cadherin bonds trigger force-activated signaling by releasing EGFR monomers to dimerize, bind EGF ligand, and signal. These findings reveal the initial steps in E-cadherin-mediated force transduction that directly link intercellular force fluctuations to the activation of growth regulatory signaling cascades." @default.
• W4210368427 created "2022-02-08" @default.
• W4210368427 creator A5000748364 @default.
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• W4210368427 date "2022-01-24" @default.
• W4210368427 modified "2023-10-10" @default.
• W4210368427 title "Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor–dependent signaling" @default.
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• W4210368427 doi "https://doi.org/10.1073/pnas.2100679119" @default.
• W4210368427 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35074920" @default.
• W4210368427 hasPublicationYear "2022" @default.
• W4210368427 type Work @default.
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• W4210368427 hasAuthorship W4210368427A5027148995 @default.

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