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- W2891447783 abstract "The response of cells to mechanical inputs is a key determinant of cell behavior. In response to external forces, E-cadherin initiates signal transduction cascades that allow the cell to modulate its contractility to withstand the force. Much attention has focused on identifying the E-cadherin signaling pathways that promote contractility, but the negative regulators remain undefined. In this study, we identify SHP-2 as a force-activated phosphatase that negatively regulates E-cadherin force transmission by dephosphorylating vinculin Y822. To specifically probe a role for SHP-2 in E-cadherin mechanotransduction, we mutated vinculin so that it retains its phosphorylation but cannot be dephosphorylated. Cells expressing the mutant vinculin have increased contractility. This work provides a mechanism for inactivating E-cadherin mechanotransduction and provides a new method for specifically targeting the action of phosphatases in cells." @default.
- W2891447783 created "2018-09-27" @default.
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- W2891447783 date "2018-01-01" @default.
- W2891447783 modified "2023-09-23" @default.
- W2891447783 title "SHP-2 is activated in response to force on E-cadherin and dephosphorylates vinculin Y822" @default.
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- W2891447783 doi "https://doi.org/10.1242/jcs.216648" @default.
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