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ß-Catenin Interacts with Low-Molecular-Weight Protein Tyrosine Phosphatase Leading to Cadherin-mediated Cell-Cell Adhesion Increase¹

Dipartimento di Scienze Biochimiche [M. L. T., P. Ch., P. Ci., F. B., T. F., E. G., D. T., G. C., G. Rau., G. Ram.], and Dipartimento di Anatomia, Istologia e Medicina Legale [L. F.], Università degli Studi di Firenze, 50134 Florence, Italy

ß-catenin plays a dual role as a major constituent of cadherin-based adherens junctions and also as a transcriptional coactivator. In normal ephitelial cells, at adherens junction level, ß-catenin links cadherins to the actin cytoskeleton. The structure of adherens junctions is dynamically regulated by tyrosine phosphorylation. In particular, cell-cell adhesion can be negatively regulated through the tyrosine phosphorylation of ß-catenin. Furthermore, the loss of ß-catenin-cadherin association has been correlated with the transition from a benign tumor to an invasive, metastatic cancer. Low-molecular-weight protein tyrosine phosphatase (LMW-PTP) is a ubiquitous PTP implicated in the regulation of mitosis and cytoskeleton rearrangement. Here we demonstrate that the amount of free cytoplasmic ß-catenin is decreased in NIH3T3, which overexpresses active LMW-PTP, and this results in a stronger association between cadherin complexes and the actin-based cytoskeleton with respect to control cells. Confocal microscopy analysis shows that ß-catenin colocalizes with LMW-PTP at the plasmamembrane. Furthermore, we provide evidence that ß-catenin is able to associate with LMW-PTP both in vitro and in vivo. Moreover, overexpression of active LMW-PTP strongly potentiates cadherin-mediated cell-cell adhesion, whereas a dominant-negative form of LMW-PTP induces the opposite phenotype, both in NIH3T3 and in MCF-7 carcinoma cells. On the basis of these results, we propose that the stability of cell-cell contacts at the adherens junction level is positively influenced by LMW-PTP expression, mainly because of the ß-catenin and LMW-PTP interaction at the plasmamembrane level with consequent dephosphorylation.

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