Journal
JOURNAL OF CELL SCIENCE
Volume 125, Issue 18, Pages 4362-4371Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.105775
Keywords
Cadherin; Mechanotransduction; Binding selectivity; Magnetic twisting cytometry; Micropipette manipulation; MTC
Categories
Funding
- National Science Foundation division of Civil, Mechanical and Manufacturing Innovation [1029871]
- National Institutes of Health [GM072744]
- National Science Foundation Integrative Graduate Education and Research Traineeship [0965918]
- National Science Foundation Chemical, Bioengineering, Environmental, and Transport Systems [0853705]
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [0853705] Funding Source: National Science Foundation
- Directorate For Engineering
- Div Of Civil, Mechanical, & Manufact Inn [1029871] Funding Source: National Science Foundation
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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. 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.
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