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Related Experiment Videos

Rap1 regulates E-cadherin-mediated cell-cell adhesion.

Leo S Price1, Amra Hajdo-Milasinovic, Jun Zhao

  • 1Department of Physiological Chemistry and the Centre for Biomedical Genetics, University Medical Centre Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands. l.s.price@med.uu.nl

The Journal of Biological Chemistry
|May 29, 2004
PubMed
Summary
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The small GTPase Rap regulates cell-cell adhesion in epithelial cells, independent of its known role in cell-matrix adhesion. Rap signaling promotes cadherin-mediated contacts, crucial for maintaining epithelial tissue structure.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The small GTPase Rap is recognized for regulating integrin-mediated cell adhesion.
  • Its precise mechanism and broader roles in cell surface receptor function remain unclear.

Purpose of the Study:

  • To investigate the role of Rap signaling in cadherin-mediated cell-cell adhesion.
  • To determine if Rap's influence on cell adhesion is independent of integrin signaling.

Main Methods:

  • Utilized Ras-transformed Madin-Darby canine kidney cells.
  • Manipulated Rap1A expression and activated endogenous Rap via Epac1.
  • Assessed cadherin-mediated cell-cell contacts and adherens junction stability.
  • Tested cell adhesion to E-cadherin in the absence of integrins.

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Main Results:

  • Constitutively active Rap1A expression restored cadherin-mediated contacts and epithelial phenotype.
  • Epac1-mediated Rap activation counteracted disruption of adherens junctions.
  • Rap signaling inhibition disrupted epithelial cell-cell contacts.
  • Rap activity was essential for cell adhesion to E-cadherin domains, independent of integrins.

Conclusions:

  • Rap signaling positively regulates cadherin-mediated cell-cell adhesion.
  • This function of Rap is independent of its effects on integrin-mediated adhesion.
  • Rap may broadly regulate various cell-surface adhesion receptors.