Force generated by actomyosin contraction builds bridges between adhesive contacts

Olivier M. Rossier, Nils Gauthier, Nicolas Biais, Wynn Vonnegut, Marc Antoine Fardin, Philip Avigan, Evan R. Heller, Anurag Mathur, Saba Ghassemi, Michael S. Koeckert, James C. Hone, Michael P. Sheetz

Research output: Contribution to journalArticlepeer-review

94 Scopus citations


Extracellular matrices in vivo are heterogeneous structures containing gaps that cells bridge with an actomyosin network. To understand the basis of bridging, we plated cells on surfaces patterned with fibronectin (FN)-coated stripes separated by non-adhesive regions. Bridges developed large tensions where concave cell edges were anchored to FN by adhesion sites. Actomyosin complexes assembled near those sites (both actin and myosin filaments) and moved towards the centre of the non-adhesive regions in a treadmilling network. Inhibition of myosin-II (MII) or Rho-kinase collapsed bridges, whereas extension continued over adhesive areas. Inhibition of actin polymerization (latrunculin-A, jasplakinolide) also collapsed the actomyosin network. We suggest that MII has distinct functions at different bridge regions: (1) at the concave edges of bridges, MIIA force stimulates actin filament assembly at adhesions and (2) in the body of bridges, myosin cross-links actin filaments and stimulates actomyosin network healing when breaks occur. Both activities ensure turnover of actin networks needed to maintain stable bridges from one adhesive region to another.

Original languageEnglish (US)
Pages (from-to)1055-1068
Number of pages14
JournalEMBO Journal
Issue number6
StatePublished - Mar 2010
Externally publishedYes


  • Actomyosin dynamics
  • Adhesion
  • Contractile treadmilling
  • Latrunculin
  • Patterned surfaces

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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