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- W1966503254 abstract "The downregulation of E-cadherin function has fundamental consequences with respect to cancer progression, and occurs as part of the epithelial–mesenchymal transition (EMT). In this study, we show that the expression of the Discosoma sp. red fluorescent protein (DsRed)-tagged cadherin cytoplasmic domain in cells inhibited the cell surface localization of endogenous E-cadherin, leading to morphological changes, the inhibition of junctional assembly and cell dissociation. These changes were associated with increased cell migration, but were not accompanied by the down-regulation of epithelial markers and up-regulation of mesenchymal markers. Thus, these changes cannot be classified as EMT. The cadherin cytoplasmic domain interacted with β-catenin or plakoglobin, reducing the levels of β-catenin or plakoglobin associated with E-cadherin, and raising the possibility that β-catenin and plakoglobin sequestration by these constructs induced E-cadherin intracellular localization. Accordingly, a cytoplasmic domain construct bearing mutations that weakened the interactions with β-catenin or plakoglobin did not impair junction formation and adhesion, indicating that the interaction with β-catenin or plakoglobin was essential to the potential of the constructs. E-cadherin–α-catenin chimeras that did not require β-catenin or plakoglobin for their cell surface transport restored cell–cell adhesion and junction formation." @default.
- W1966503254 created "2016-06-24" @default.
- W1966503254 creator A5012371668 @default.
- W1966503254 creator A5068682184 @default.
- W1966503254 date "2014-08-14" @default.
- W1966503254 modified "2023-10-17" @default.
- W1966503254 title "Cadherin Cytoplasmic Domains Inhibit the Cell Surface Localization of Endogenous E-Cadherin, Blocking Desmosome and Tight Junction Formation and Inducing Cell Dissociation" @default.
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- W1966503254 doi "https://doi.org/10.1371/journal.pone.0105313" @default.
- W1966503254 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4133371" @default.
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