Author:
Tabdili Hamid,Langer Matthew,Shi Quanming,Poh Yeh-Chuin,Wang Ning,Leckband Deborah
Abstract
This study investigates the relationship between classical cadherin binding affinities and mechanotransduction through cadherin-mediated 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. Here, micropipette measurements quantified the two-dimensional affinities of cadherins at the cell surface, and two complementary mechanical measurements assessed 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 three fold. In contrast, mechanotransduction via 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.
Publisher
The Company of Biologists
Cited by
50 articles.
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