Deletion of the cytoplasmic domain of N-cadherin reduces, but does not eliminate, traction force-transmission

Eliot Lee, Makena L. Ewald, Mary Sedarous, Timothy Kim, Brent W. Weyers, Rose Hong Truong, Soichiro Yamada

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Collective migration of epithelial cells is an integral part of embryonic development, wound healing, tissue renewal and carcinoma invasion. While previous studies have focused on cell-extracellular matrix adhesion as a site of migration-driving, traction force-transmission, cadherin mediated cell-cell adhesion is also capable of force-transmission. Using a soft elastomer coated with purified N-cadherin as a substrate and a Hepatocyte Growth Factor-treated, transformed MDCK epithelial cell line as a model system, we quantified traction transmitted by N-cadherin-mediated contacts. On a substrate coated with purified extracellular domain of N-cadherin, cell surface N-cadherin proteins arranged into puncta. N-cadherin mutants (either the cytoplasmic deletion or actin-binding domain chimera), however, failed to assemble into puncta, suggesting the assembly of focal adhesion like puncta requires the cytoplasmic domain of N-cadherin. Furthermore, the cytoplasmic domain deleted N-cadherin expressing cells exerted lower traction stress than the full-length or the actin binding domain chimeric N-cadherin. Our data demonstrate that N-cadherin junctions exert significant traction stress that requires the cytoplasmic domain of N-cadherin, but the loss of the cytoplasmic domain does not completely eliminate traction force transmission.

Original languageEnglish (US)
Pages (from-to)1640-1646
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Sep 30 2016


  • Actin cytoskeleton
  • Collective cell migration
  • Hepatocyte Growth Factor
  • MDCK
  • N-cadherin
  • Traction force

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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