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Updated: Jul 6, 2026
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Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
Published on: November 2, 2011
Beyond structure: mechanism and dynamics of intercellular adhesion.
1Department of Chemistry, Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA. Leckband@scs.uiuc.edu
Biochemical Society Transactions
|March 28, 2008
Summary
Classical cadherins use a multistage binding mechanism involving multiple extracellular domains for cell adhesion. This process transitions from weak, fast binding to strong, slow binding, revealing a complex adhesion model.
Area of Science:
- Cellular Biology
- Biophysics
- Molecular Biology
Background:
- Classical cadherins are crucial for cell-cell adhesion.
- Understanding cadherin binding mechanisms is vital for cell biology.
Purpose of the Study:
- To review quantitative investigations on classical cadherin adhesion.
- To elucidate the multistage binding mechanism of cadherins.
Main Methods:
- Quantitative investigations from single molecules to cells.
- Kinetic, energetic, and mechanical strength measurements of cadherin bonds.
Main Results:
- Cadherin adhesion involves a multistage mechanism with multiple extracellular domains.
- Cell adhesion exhibits a two-stage process: initial weak binding followed by strong binding.
- N-terminal domains mediate initial binding; EC3 and full ectodomain are key for strong binding.
Conclusions:
- Cadherin adhesion is a complex, multistage process.
- Binding mechanism is more intricate than previously suggested by structural models.
- This mechanism is independent of the cytoplasmic domain.
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