Robert W. McLachlan

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Cell-cell contacts are major determinants of tissue organization in both health and disease. Adhesive interactions, especially those mediated by classical cadherin receptors, influence cell-cell recognition and tissue patterning during development. Conversely, cadherin dysfunction promotes tumor progression to invasion and metastasis. Over the past three(More)
Src family kinases (SFKs) signal in response to E-cadherin to support cadherin adhesion and the integrity of cell-cell contacts (McLachlan, R. W., Kraemer, A., Helwani, F. M., Kovacs, E. M., and Yap, A. S. (2007) Mol. Biol. Cell 18, 3214-3223). We now identify the actin-regulatory protein, cortactin, as a target of E-cadherin-activated SFK signaling.(More)
Co-operation between cadherin adhesion molecules and the cytoskeleton is a key aspect of tissue morphogenesis that is mediated by cortical signaling at adhesive junctions. One such signal is the non-receptor tyrosine kinase, Src, which acts in several pathways at epithelial junctions, including E-cadherin signaling itself. We now present two new insights(More)
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(More)
Cadherin cell-cell adhesion critically determines tissue organization and integrity in many organs of the body. Cadherin function influences patterning and morphogenesis while cadherin dysfunction contributes to disease, notably tumor invasion and metastasis. Cell signaling events are intimately linked with cadherin function; it is increasingly apparent(More)
Cell-cell adhesion couples the contractile cortices of epithelial cells together, generating tension to support a range of morphogenetic processes. E-cadherin adhesion plays an active role in generating junctional tension by promoting actin assembly and cortical signaling pathways that regulate myosin II. Multiple myosin II paralogues accumulate at(More)
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