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Updated: Jul 14, 2026
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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
Published on: October 17, 2014
E-cadherin adhesion activates c-Src signaling at cell-cell contacts
Robert W McLachlan1, Astrid Kraemer, Falak M Helwani
1Division of Molecular Cell Biology, Institute for Molecular Bioscience, The University of Queensland, St. Lucia, Brisbane, Queensland, Australia 4072.
Molecular Biology of the Cell
|June 8, 2007
Summary
Cadherin adhesion activates c-Src signaling, which supports cell-cell contact function at low levels but inhibits it at high levels. This pathway involves PI3-kinase signaling.
Area of Science:
- Cell biology
- Molecular signaling
- Biochemistry
Background:
- Cadherin-based cell-cell contacts are crucial for tissue integrity and are enriched in phosphotyrosine signaling components.
- The precise interplay between cadherin adhesion and tyrosine kinase signaling remains incompletely understood.
Purpose of the Study:
- To investigate whether cadherin adhesion activates c-Src signaling.
- To determine the impact of c-Src signaling on cadherin function.
Main Methods:
- Studied signaling pathways activated by cadherin receptor ligation.
- Assessed cadherin function under varying c-Src signaling strengths.
- Investigated the role of PI3-kinase signaling in the observed effects.
Main Results:
- Cadherin adhesion activates c-Src signaling.
- c-Src exhibits a biphasic effect on cadherin function: supportive at low signal strengths, inhibitory at high signal strengths.
- Inhibition of c-Src reduced cadherin function when activated by adhesion.
- PI3-kinase signaling is implicated as a downstream target of cadherin-activated c-Src, contributing to its positive effects.
Conclusions:
- E-cadherin signaling activates c-Src at cell-cell contacts, influencing cadherin function.
- The signaling pathway provides a key input where signal strength quantitatively modulates functional outcomes.
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