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Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion

Hajime Yano1, Yuichi Mazaki, Kazuo Kurokawa

  • 1Department of Molecular Biology, Osaka Bioscience Institute, Osaka 565-0874, Japan.

The Journal of Cell Biology
|July 21, 2004
PubMed

Insights

Integrin signaling molecules like Fak and paxillin regulate N-cadherin cell-cell adhesion. Fak signaling down-regulates Rac1 activity, crucial for cell migration in development and cancer.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrins and cadherins are cell adhesion molecules with known crosstalk.
  • Understanding their interplay is crucial for cell migration and tissue development.

Purpose of the Study:

  • To investigate the relationship between integrin signaling and N-cadherin-mediated cell-cell adhesion.
  • To identify specific integrin signaling molecules involved in regulating N-cadherin function.

Main Methods:

  • Utilized small interfering RNA (siRNA) for targeted protein knockdown in HeLa cells.
  • Analyzed the impact of knockdown on focal adhesions and cell-cell adhesion formation.
  • Investigated the role of specific signaling molecules, including Fak and paxillin.

Main Results:

  • Fak and paxillin, but not p130Cas or Pyk2, were found to regulate N-cadherin adhesion.
  • Paxillin is essential for recruiting Fak to focal adhesions.
  • Fak signaling down-regulates Rac1 activity at the cell periphery, promoting N-cadherin adhesion formation.
  • Fak plays a critical role in maintaining cell-cell adhesion during collective cell migration.

Conclusions:

  • Integrin signaling, particularly through Fak and paxillin, directly influences N-cadherin-based cell-cell adhesion.
  • The Fak-Rac1 pathway is a key regulator of N-cadherin adhesion in motile cells.
  • These findings highlight the importance of Fak in collective cell migration during embryonic development and cancer invasion.

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