<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Fournier MF</dc:creator>
  <dc:creator>Sauser R</dc:creator>
  <dc:creator>Ambrosi D</dc:creator>
  <dc:creator>Meister JJ</dc:creator>
  <dc:creator>Verkhovsky AB</dc:creator>
  <dc:date>2010</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">During cell migration, forces generated by the actin cytoskeleton are transmitted through adhesion complexes to the substrate. To investigate the mechanism of force generation and transmission, we analyzed the relationship between actin network velocity and traction forces at the substrate in a model system of persistently migrating fish epidermal keratocytes. Front and lateral sides of the cell exhibited much stronger coupling between actin motion and traction forces than the trailing cell body. Further analysis of the traction-velocity relationship suggested that the force transmission mechanisms were different in different cell regions: at the front, traction was generated by a gripping of the actin network to the substrate, whereas at the sides and back, it was produced by the network's slipping over the substrate. Treatment with inhibitors of the actin-myosin system demonstrated that the cell body translocation could be powered by either of the two different processes, actomyosin contraction or actin assembly, with the former associated with significantly larger traction forces than the latter.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/48596</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1083/jcb.200906139</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/20100912</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>The Journal of cell biology. - 2010</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Actin Cytoskeleton</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Biomechanical Phenomena</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Cell Adhesion</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Cell Movement</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Cell Polarity</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Cell Shape</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Cells, Cultured</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Cytochalasin D</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Cytoskeleton</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Fishes</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Heterocyclic Compounds, 4 or More Rings</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Keratinocytes</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Models, Biological</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Myosins</dc:subject>
  <dc:subject xmlns:ns16="xml" ns16:lang="en">Protein Synthesis Inhibitors</dc:subject>
  <dc:subject xmlns:ns17="xml" ns17:lang="en">Stress, Mechanical</dc:subject>
  <dc:subject xmlns:ns18="xml" ns18:lang="en">Tensile Strength</dc:subject>
  <dc:title xmlns:ns19="xml" ns19:lang="en">Force transmission in migrating cells.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
