SHP-2 is activated in response to force on E-cadherin and dephosphorylates vinculin Y822

J Cell Sci. 2018 Dec 14;131(24):jcs216648. doi: 10.1242/jcs.216648.

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.

Keywords: Cell stiffening; E-cadherin; Force; SHP-2; Vinculin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Cadherins / metabolism*
  • Cell Adhesion / physiology
  • Cytoskeleton / metabolism
  • Humans
  • Mechanotransduction, Cellular / physiology
  • Phosphorylation
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11 / metabolism*
  • Vinculin / metabolism*
  • alpha Catenin / metabolism*

Substances

  • Actins
  • Cadherins
  • VCL protein, human
  • alpha Catenin
  • Vinculin
  • PTPN11 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11