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The E‐cadherin/epidermal growth factor receptor interaction: a hypothesis of reciprocal and reversible control of intercellular adhesion and cell proliferation
Author(s) -
Jawhari Aida U.,
Farthing Michael J. G.,
Pignatelli Massimo
Publication year - 1999
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/(sici)1096-9896(199901)187:2<155::aid-path193>3.0.co;2-e
Subject(s) - adherens junction , cadherin , microbiology and biotechnology , catenin , biology , tyrosine phosphorylation , cell adhesion , actin cytoskeleton , epidermal growth factor , cell adhesion molecule , epidermal growth factor receptor , phosphorylation , cytoskeleton , signal transduction , receptor , cell , wnt signaling pathway , biochemistry
The E‐cadherin/catenin complex is a calcium‐dependent cell–cell adhesion molecule, whose function is critical to the integrity of the adherens junction and which plays a role in the establishment and maintenance of normal epithelial morphology and differentiation. Loss of E‐cadherin‐mediated adhesion appears to be a fundamental aspect of the neoplastic phenotype which in some cases appears to be mediated by post‐translational modifications (i.e. tyrosine phosphorylation) of its interacting proteins, the catenins which link E‐cadherin to the actin cytoskeleton. There is increasing experimental evidence to suggest that epidermal growth factor receptor tyrosine phosphorylation may lead to the inactivation of the E‐cadherin/catenin complex in cancer cells through its interaction with β‐ or γ‐ catenin in the cytoskeleton. Modulation of epidermal growth factor receptor activity by pharmacological agents has the potential to regulate a variety of cellular processes including adhesion, differentiation, and proliferation. Copyright © 1999 John Wiley & Sons, Ltd.