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Adhesive and lateral E-cadherin dimers are mediated by the same interface.
Regina B Troyanovsky1, Eugene Sokolov, Sergey M Troyanovsky
1Division of Dermatology, Washington University Medical School, 660 S. Euclid Avenue, St. Louis, MO 63110, USA.
Molecular and Cellular Biology
|October 31, 2003
Summary
E-cadherin forms adhesive dimers crucial for cell adhesion. Calcium levels influence dimer formation, revealing structural flexibility in the extracellular cadherin region.
Area of Science:
- Cell Biology
- Biochemistry
- Structural Biology
Background:
- E-cadherin is a key transmembrane protein mediating calcium-dependent cell-cell adhesion.
- Understanding cadherin-cadherin interactions is vital for elucidating the molecular mechanisms of cell adhesion.
Purpose of the Study:
- To investigate E-cadherin dimerization and its structural basis.
- To explore the role of specific cysteine mutations in revealing cadherin-cadherin interactions.
- To differentiate between adhesive and lateral E-cadherin dimers.
Main Methods:
- Expression of recombinant wild-type E-cadherin and cysteine mutants in A-431 cells.
- Utilizing the bifunctional cross-linker BM(PE0)3 to detect E-cadherin dimers.
- Employing co-immunoprecipitation assays to characterize dimer properties.
Main Results:
- Cysteine mutations at strand B of the EC1 domain successfully induced E-cadherin dimerization.
- Adhesive dimers are the dominant form under standard culture conditions.
- Calcium depletion dissociates adhesive dimers and promotes the formation of lateral dimers.
- Both dimer types are mediated by the amino-terminal cadherin domain and share similar interfaces.
Conclusions:
- E-cadherin dimerization is mediated by its amino-terminal domain.
- The extracellular cadherin region exhibits flexibility, allowing for the coexistence of structurally identical adhesive and lateral dimers.
- Calcium availability dynamically regulates the formation of different E-cadherin dimer interfaces.