Abstract
We found that E-cadherin and epidermal growth factor receptor (EGFR) are associated in mammary epithelial cells and that E-cadherin engagement in these cells induces transient activation of EGFR, as previously seen in keratinocytes (37). In contrast, EGFR does not associate with and is not activated by N-cadherin. Analysis of cells expressing chimeric cadherins revealed that the extracellular domain of E-cadherin is required for interaction with and activation of EGFR. This activation results in tyrosine phosphorylation of known EGFR substrates and reduction in focal adhesions. These interactions, however, are not necessary for suppression of cell motility by E-cadherin.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Breast Neoplasms / genetics
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Breast Neoplasms / metabolism
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Cadherins / genetics
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Cadherins / metabolism*
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Carcinoma / genetics
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Carcinoma / metabolism
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Cell Adhesion / genetics
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Cell Line, Tumor
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Cell Movement / genetics
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Cell Transformation, Neoplastic / genetics
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Epithelial Cells / cytology
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Epithelial Cells / metabolism*
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ErbB Receptors / metabolism*
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Focal Adhesions / genetics
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Focal Adhesions / metabolism
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Gene Expression Regulation, Neoplastic / genetics
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Humans
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Mammary Glands, Human / cytology
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Mammary Glands, Human / metabolism*
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Neoplasm Metastasis / genetics
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Phosphorylation
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Protein Structure, Tertiary / genetics
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Up-Regulation / genetics
Substances
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Cadherins
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Recombinant Fusion Proteins
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ErbB Receptors