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J Biol Chem, Vol. 274, Issue 15, 10173-10183, April 9, 1999
-Catenin Are Regulated by
Tyrosine Kinases and Tyrosine Phosphatases during Epithelial Cell
Migration
,,
From the Cell migration requires precise control, which is
altered or lost when tumor cells become invasive and metastatic.
Although the integrity of cell-cell contacts, such as adherens
junctions, is essential for the maintenance of functional epithelia,
they need to be rapidly disassembled during migration. The
transmembrane cell adhesion protein E-cadherin and the cytoplasmic
catenins are molecular elements of these structures. Here we
demonstrate that epithelial cell migration is accompanied by tyrosine
phosphorylation of Department of Molecular Biology, Max Planck
Institute for Biochemistry, Am Klopferspitz 18a, 82152 Martinsried,
Federal Republic of Germany and ¶ Swiss Institute for Experimental
Cancer Research (ISREC), Chemin des Boveresses 155, 1066 Epalinges, Switzerland
-catenin and an increase of its free cytoplasmic
pool. We show further that the protein-tyrosine phosphatase LAR
(leukocyte common antigen related) colocalizes with the
cadherin-catenin complex in epithelial cells and associates with
-catenin and plakoglobin. Interestingly, ectopic expression of
protein-tyrosine phosphatase (PTP) LAR inhibits epithelial cell
migration by preventing phosphorylation and the increase in the free
pool of -catenin; moreover, it inhibits tumor formation in nude
mice. These data support a function for PTP LAR in the regulation of
epithelial cell-cell contacts at adherens junctions as well as in the
control of -catenin signaling functions. Thus PTP-LAR appears to
play an important role in the maintenance of epithelial integrity, and
a loss of its regulatory function may contribute to malignant progression and metastasis.
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