α-Catenin and Vinculin Cooperate to Promote High E-cadherin-based Adhesion Strength

Thomas, William A.; Boscher, Cécile; Chu, Yu‐Xia; Cuvelier, Damien; Martinez-Rico, Clara; Seddiki, Rima; Heysch, Julie; Ladoux, Benoît; Thiery, Jean Paul; Mège, René Marc; Dufour, Sylvie

doi:10.1074/jbc.m112.403774

Cited by 157 publications

(166 citation statements)

References 59 publications

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“…This study aligns with the important fi nding that α -catenin undergoes a conformational change allowing for vinculin binding and consequently AJ stability and force transmission (Yonemura et al, 2010). In a related dual pipette study, Thomas et al (2013) found that overexpression of mutant forms of the α -catenin vinculin-binding domain or depletion of vinculin signifi cantly reduced adhesion strength of S180 cells and that localization of vinculin was dependent on the stretching of, or increasing the force between cells in the assay. Such fi ndings provide evidence that the mechanotransductive properties of cadherin adhesions may be modulated by the cytoplasmic complex through which cadherins are linked to the actin cytoskeleton.…”

Section: Forces Between Cells In 2d Culturesupporting

confidence: 81%

Force Measurement Tools to Explore Cadherin Mechanotransduction

Stapleton

Chopra

Chen

2014

Cell Communication & Adhesion

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Cell -cell adhesions serve to mechanically couple cells, allowing for long-range transmission of forces across cells in development, disease, and homeostasis. Recent work has shown that such contacts also play a role in transducing mechanical cues into a wide variety of cellular behaviors important to tissue function. As such, understanding the mechanical regulation of cells through their adhesion molecules has become a point of intense focus. This review will highlight the existing and emerging technologies and models that allow for exploration of cadherin-based adhesions as sites of mechanotransduction.

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Section: Forces Between Cells In 2d Culturesupporting

confidence: 81%

Force Measurement Tools to Explore Cadherin Mechanotransduction

Stapleton

Chopra

Chen

2014

Cell Communication & Adhesion

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“…By showing RPTPa-mediated regulation of the junctional cortactin pool, our studies thus implicate RPTPa in coordination between E-cadherin and the actin cytoskeleton, a crucial process for intercellular adhesion (Lambert et al, 2002;Thomas et al, 2013).…”

Section: (Five Independent Experiments) (B)mentioning

confidence: 55%

Receptor protein tyrosine phosphatase RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src signaling to cortactin

Truffi

Dubreuil

Liang

et al. 2014

Journal of Cell Science

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Epithelial junctions are fundamental determinants of tissue organization, subject to regulation by tyrosine phosphorylation. Homophilic binding of E-cadherin activates tyrosine kinases, such as Src, that control junctional integrity. Protein tyrosine phosphatases (PTPs) also contribute to cadherin-based adhesion and signaling, but little is known about their specific identity or functions at epithelial junctions. Here, we report that the receptor PTP RPTPa (human gene name PTPRA) is recruited to epithelial adherens junctions at the time of cell-cell contact, where it is in molecular proximity to E-cadherin. RPTPa is required for appropriate cadherin-dependent adhesion and for cyst architecture in three-dimensional culture. Loss of RPTPa impairs adherens junction integrity, as manifested by defective E-cadherin accumulation and peri-junctional F-actin density. These effects correlate with a role for RPTPa in cellular (c)-Src activation at sites of E-cadherin engagement. Mechanistically, RPTPa is required for appropriate tyrosine phosphorylation of cortactin, a major Src substrate and a cytoskeletal actin organizer. Expression of a phosphomimetic cortactin mutant in RPTPa-depleted cells partially rescues F-actin and E-cadherin accumulation at intercellular contacts. These findings indicate that RPTPa controls cadherinmediated signaling by linking homophilic E-cadherin engagement to cortactin tyrosine phosphorylation through c-Src.

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“…The strengthening of cadherin-mediated intercellular adhesion has been attributed to several mechanisms, including GTPase activity (27)(28)(29)(30)(31), enhanced cadherin-cytoskeletal interactions (5,(32)(33)(34)(35), cadherin catch bonds (36), cadherin clustering (19,37,38), and altered cortical tension (5,6). Demonstrating that Colo 205 aggregation was caused by the allosteric regulation of E-cadherin required a demonstration that specific perturbations, which do not affect the binding site directly, caused quantitative changes in the E-cadherin affinity.…”

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confidence: 99%

Allosteric Regulation of E-Cadherin Adhesion

Shashikanth¹,

Petrova

Park³

et al. 2015

Journal of Biological Chemistry

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Background: Measured binding kinetics between Colo 205 cells tested the postulate that E-cadherin adhesion is allosterically regulated. Results: p120 catenin dephosphorylation or cell treatment with activating anti-E-cadherin antibody increased E-cadherin binding affinities by 2-3-fold. Conclusion: Perturbations that do not directly affect the binding site enhanced the adhesive function of E-cadherin. Significance: These biophysical measurements demonstrated that E-cadherin is allosterically regulated.

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α-Catenin and Vinculin Cooperate to Promote High E-cadherin-based Adhesion Strength

Cited by 157 publications

References 59 publications

Force Measurement Tools to Explore Cadherin Mechanotransduction

Force Measurement Tools to Explore Cadherin Mechanotransduction

Receptor protein tyrosine phosphatase RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src signaling to cortactin

Allosteric Regulation of E-Cadherin Adhesion

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