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Related Experiment Videos

Structure-function analysis of cell adhesion by neural (N-) cadherin

K Tamura1, W S Shan, W A Hendrickson

  • 1Brookdale Center for Developmental and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029, USA.

Neuron
|July 9, 1998
PubMed
Summary

Site-directed mutagenesis reveals that the N-cadherin strand dimer interface is crucial for cell adhesion. This suggests cadherins may exist in monomeric and dimeric forms, with the strand dimer potentially activating adhesion.

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Area of Science:

  • Cell adhesion
  • Structural biology
  • Molecular biology

Background:

  • Cadherins mediate cell-cell adhesion, crucial for tissue development and integrity.
  • The lateral "strand dimer" in N-cadherin's D1 domain has an unknown biological function.
  • Previous studies suggest cadherin dimerization/clustering enhances adhesion.

Purpose of the Study:

  • To investigate the biological role of the N-cadherin strand dimer.
  • To explore the structural basis of cadherin-mediated cell adhesion.

Main Methods:

  • Site-directed mutagenesis of N-cadherin and E-cadherin.
  • Cell adhesion assays.
  • Crystal structure determination of a Ca2+-complexed N-cadherin fragment.

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Main Results:

  • Mutations at the strand dimer interface abolish N-cadherin's cell adhesion ability.
  • A similar mutation in E-cadherin also abrogates its adhesive capacity.
  • The crystal structure of a Ca2+-bound N-cadherin fragment does not show the strand dimer conformation, suggesting stable monomeric and dimeric forms.

Conclusions:

  • The strand dimer interface is essential for classical cadherin-mediated cell adhesion.
  • Classical cadherins may exist in both monomeric and dimeric states.
  • The strand dimer might play a role in activating cadherin adhesion, potentially through lateral dimerization or clustering.