E-Cadherin Adhesion Activates c-Src Signaling at Cell-Cell contacts

McLachlan, R. W., Kraemer, A., Helwani, F. M., Kovacs, E. M. and Yap, Alpha S. K. (2007) E-Cadherin Adhesion Activates c-Src Signaling at Cell-Cell contacts. Molecular Biology of the Cell, 18 8: 3214-3223. doi:10.1091/mbc.E06-12-1154

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Author McLachlan, R. W.
Kraemer, A.
Helwani, F. M.
Kovacs, E. M.
Yap, Alpha S. K.
Title E-Cadherin Adhesion Activates c-Src Signaling at Cell-Cell contacts
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2007-08
Sub-type Article (original research)
DOI 10.1091/mbc.E06-12-1154
Open Access Status File (Publisher version)
Volume 18
Issue 8
Start page 3214
End page 3223
Total pages 10
Editor Schmid, S.L.
Place of publication Bethesda, MD
Publisher American Society for Cell Biology
Collection year 2008
Language eng
Subject C1
270105 Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)
780105 Biological sciences
Abstract Cadherin-based cell-cell contacts are prominent sites for phosphotyrosine signaling, being enriched in tyrosine-phosphorylated proteins and tyrosine kinases and phosphatases. The functional interplay between cadherin adhesion and tyrosine kinase signaling, however, is complex and incompletely understood. In this report we tested the hypothesis that cadherin adhesion activates c-Src signaling and sought to assess its impact on cadherin function. We identified c-Src as part of a cadherin-activated cell signaling pathway that is stimulated by ligation of the adhesion receptor. However, c-Src has a biphasic impact on cadherin function, exerting a positive supportive role at lower signal strengths, but inhibiting function at high signal strengths. Inhibiting c-Src under circumstances when it is activated by cadherin adhesion decreased several measures of cadherin function. This suggests that the cadherin-activated c-Src signaling pathway serves positively to support cadherin function. Finally, our data implicate PI3-kinase signaling as a target for cadherin-activated c-Src signaling that contributes to its positive impact on cadherin function. We conclude that E-cadherin signaling is an important activator of c-Src at cell-cell contacts, providing a key input into a signaling pathway where quantitative changes in signal strength may result in qualitative differences in functional outcome.
Keyword Cell Biology
Tyrosine Phosphorylation
Phosphatidylinositol 3-kinase
V-src
Local Concentration
Family Kinases
Junctions
Complex
Rac
Drosophila
P120(ctn)
Q-Index Code C1
Q-Index Status Confirmed Code

 
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Created: Thu, 10 Apr 2008, 09:32:45 EST by Jennifer Greder on behalf of Institute for Molecular Bioscience