E-cadherin binding modulates EGF receptor activation
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...
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Veröffentlicht in: | Cell communication & adhesion 2003-03, Vol.10 (2), p.105-118 |
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creator | Fedor-Chaiken, Mary Hein, Patrick W Stewart, Jane C Brackenbury, Robert Kinch, Michael S |
description | 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. |
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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.</description><subject>Breast Neoplasms - genetics</subject><subject>Breast Neoplasms - metabolism</subject><subject>Cadherins - genetics</subject><subject>Cadherins - metabolism</subject><subject>Carcinoma - genetics</subject><subject>Carcinoma - metabolism</subject><subject>Cell Adhesion - genetics</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement - genetics</subject><subject>Cell Transformation, Neoplastic - genetics</subject><subject>Epithelial Cells - cytology</subject><subject>Epithelial Cells - metabolism</subject><subject>Focal Adhesions - genetics</subject><subject>Focal Adhesions - metabolism</subject><subject>Gene Expression Regulation, Neoplastic - genetics</subject><subject>Humans</subject><subject>Mammary Glands, Human - cytology</subject><subject>Mammary Glands, Human - metabolism</subject><subject>Neoplasm Metastasis - genetics</subject><subject>Phosphorylation</subject><subject>Protein Structure, Tertiary - genetics</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Up-Regulation - genetics</subject><issn>1541-9061</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM1KxDAYRbNQnHF04QtIV4KL6pfmp-lShs4oDLjRdUmTLxrpn0kr-PZWpih3cTeHC_cQckXhjoKC-5xymEPlCVlTwWlagKQrch7jB0CWARdnZEW5VBQkrAkvU6PtOwbfJbXvrO_ekra3U6NHjEm53yUBDQ5jHxJtRv-lR993F-TU6Sbi5dIb8rorX7aP6eF5_7R9OKQm42pMjUJ0BXeZLlDoHFCo2tZKMcy1YnlNUXHBHLWusNIi0xqEcrnKtBDMyIxtyM1xdwj954RxrFofDTaN7rCfYjV_lYKDmMHbI2hCH2NAVw3Btzp8VxSqXy3Vn5aZvV5Gp7pF-08uTtgP3QxdlQ</recordid><startdate>200303</startdate><enddate>200303</enddate><creator>Fedor-Chaiken, Mary</creator><creator>Hein, Patrick W</creator><creator>Stewart, Jane C</creator><creator>Brackenbury, Robert</creator><creator>Kinch, Michael S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200303</creationdate><title>E-cadherin binding modulates EGF receptor activation</title><author>Fedor-Chaiken, Mary ; 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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.</abstract><cop>England</cop><pmid>14681060</pmid><doi>10.1080/714040416</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Breast Neoplasms - genetics Breast Neoplasms - metabolism Cadherins - genetics Cadherins - metabolism Carcinoma - genetics Carcinoma - metabolism Cell Adhesion - genetics Cell Line, Tumor Cell Movement - genetics Cell Transformation, Neoplastic - genetics Epithelial Cells - cytology Epithelial Cells - metabolism Focal Adhesions - genetics Focal Adhesions - metabolism Gene Expression Regulation, Neoplastic - genetics Humans Mammary Glands, Human - cytology Mammary Glands, Human - metabolism Neoplasm Metastasis - genetics Phosphorylation Protein Structure, Tertiary - genetics Receptor, Epidermal Growth Factor - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Up-Regulation - genetics |
title | E-cadherin binding modulates EGF receptor activation |
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