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PLoS One. 2016 Feb 4;11(2):e0148574. doi: 10.1371/journal.pone.0148574. eCollection 2016.

Microtubules Inhibit E-Cadherin Adhesive Activity by Maintaining Phosphorylated p120-Catenin in a Colon Carcinoma Cell Model.

Author information

1
Department of Cell Biology, University of Virginia School of Medicine, Charlottesville, Virginia, United States of America.
2
Department of Biology, Truman State University, Kirksville, Missouri, United States of America.
3
Seattle Children's Research Institute and University of Washington School of Medicine, Seattle, Washington, United States of America.

Abstract

Tight regulation of cadherin-mediated intercellular adhesions is critical to both tissue morphogenesis during development and tissue homeostasis in adults. Cell surface expression of the cadherin-catenin complex is often directly correlated with the level of adhesion, however, examples exist where cadherin appears to be inactive and cells are completely non-adhesive. The state of p120-catenin phosphorylation has been implicated in regulating the adhesive activity of E-cadherin but the mechanism is currently unclear. We have found that destabilization of the microtubule cytoskeleton, independent of microtubule plus-end dynamics, dephosphorylates p120-catenin and activates E-cadherin adhesion in Colo 205 cells. Through chemical screening, we have also identified several kinases as potential regulators of E-cadherin adhesive activity. Analysis of several p120-catenin phosphomutants suggests that gross dephosphorylation of p120-catenin rather than that of specific amino acids may trigger E-cadherin adhesion. Uncoupling p120-catenin binding to E-cadherin at the membrane causes constitutive adhesion in Colo 205 cells, further supporting an inhibitory role of phosphorylated p120-catenin on E-cadherin activity.

PMID:
26845024
PMCID:
PMC4742228
DOI:
10.1371/journal.pone.0148574
[Indexed for MEDLINE]
Free PMC Article

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