Activation of beta 1 but not beta 3 integrin increases cell traction forces

FEBS Lett. 2013 Mar 18;587(6):763-9. doi: 10.1016/j.febslet.2013.01.068. Epub 2013 Feb 8.

Abstract

Cell-generated traction forces induce integrin activation, leading to focal adhesion growth and cell spreading. It remains unknown, however, whether integrin activation feeds back to impact the generation of cytoskeletal tension. Here, we used elastomeric micropost arrays to measure cellular traction forces in wildtype and integrin-null cells. We report that activation of β1 but not β3 integrin, by either increasing density of immobilized fibronectin or treating with manganese, elicited fibroblast spreading and cytoskeletal tension. Furthermore, this force generation required Rho kinase and myosin activity. These findings suggest that integrin activation and cell traction forces comprise a bi-directional signaling unit of cell adhesion.

Publication types

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

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Line
  • Cell Movement
  • Cytoskeleton / metabolism
  • Fibroblasts / cytology
  • Fibroblasts / metabolism*
  • Fibronectins / chemistry
  • Immobilized Proteins / chemistry
  • Integrin alpha5 / genetics
  • Integrin alpha5 / metabolism
  • Integrin beta1 / genetics
  • Integrin beta1 / metabolism*
  • Integrin beta3 / genetics
  • Integrin beta3 / metabolism*
  • Manganese / metabolism
  • Mechanotransduction, Cellular*
  • Mice
  • Myosins / genetics
  • Myosins / metabolism
  • RNA, Small Interfering / genetics
  • Surface Tension
  • Up-Regulation
  • rho-Associated Kinases / genetics
  • rho-Associated Kinases / metabolism

Substances

  • Fibronectins
  • Immobilized Proteins
  • Integrin alpha5
  • Integrin beta1
  • Integrin beta3
  • RNA, Small Interfering
  • Manganese
  • rho-Associated Kinases
  • Myosins