Cadherin-dependent mechanotransduction depends on ligand identity but not affinity

Hamid Tabdili, Matthew Langer, Quanming Shi, Yeh Chuin Poh, Ning Wang, Deborah Leckband

Research output: Contribution to journalArticlepeer-review


This study investigates the relationship between classical cadherin binding affinities and mechanotransduction through cadherinmediated adhesions. The mechanical properties of cadherin-dependent intercellular junctions are generally attributed to differences in the binding affinities of classical cadherin subtypes that contribute to cohesive energies between cells. However, cell mechanics and mechanotransduction may also regulate intercellular contacts. We used micropipette measurements to quantify the two-dimensional affinities of cadherins at the cell surface, and two complementary mechanical measurements to assess ligand-dependent mechanotransduction through cadherin adhesions. At the cell surface, the classical cadherins investigated in this study form both homophilic and heterophilic bonds with two-dimensional affinities that differ by less than threefold. In contrast, mechanotransduction through cadherin adhesions is strongly ligand dependent such that homophilic, but not heterophilic ligation mediates mechanotransduction, independent of the cadherin binding affinity. These findings suggest that ligand-selective mechanotransduction may supersede differences in cadherin binding affinities in regulating intercellular contacts.

Original languageEnglish (US)
Pages (from-to)4362-4371
Number of pages10
JournalJournal of cell science
Issue number18
StatePublished - 2012


  • Binding selectivity
  • Cadherin
  • Magnetic twisting cytometry
  • Mechanotransduction
  • Micropipette manipulation
  • MTC

ASJC Scopus subject areas

  • Cell Biology


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