4.7 Article

αE-catenin regulates actin dynamics independently of cadherin-mediated cell-cell adhesion

Journal

JOURNAL OF CELL BIOLOGY
Volume 189, Issue 2, Pages 339-352

Publisher

ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200910041

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Funding

  1. Stanford Graduate Fellowship and Cancer Biology Training [5 T32 CA009151-34]
  2. Ruth L. Kirschstein National Research service award [5T32 CA09302]
  3. National Institutes of Health [GM35527, GM56169, GM70898]

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alpha E-catenin binds the cell-cell adhesion complex of E-cadherin and beta-catenin (beta-cat) and regulates filamentous actin (F-actin) dynamics. In vitro, binding of alpha E-catenin to the E-cadherin-beta-cat complex lowers alpha E-catenin affinity for F-actin, and alpha E-catenin alone can bind F-actin and inhibit Arp2/3 complex-mediated actin polymerization. In cells, to test whether alpha E-catenin regulates actin dynamics independently of the cadherin complex, the cytosolic alpha E-catenin pool was sequestered to mitochondria without affecting overall levels of alpha E-catenin or the cadherin-catenin complex. Sequestering cytosolic alpha E-catenin to mitochondria alters lamellipodia architecture and increases membrane dynamics and cell migration without affecting cell-cell adhesion. In contrast, sequestration of cytosolic alpha E-catenin to the plasma membrane reduces membrane dynamics. These results demonstrate that the cytosolic pool of alpha E-catenin regulates actin dynamics independently of cell-cell adhesion.

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