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(Received for publication, February 15, 1996, and in revised form, April 22, 1996)
From the Department of Molecular Biology, Max-Planck-Institut
für Biochemie, Am Klopferspitz 18A, 82152 Martinsried, Federal
Republic of Germany
We have identified a human receptor-like
protein-tyrosine phosphatase (PTP) in the mammary carcinoma cell line
SK-BR-3, which represents the human homolog of murine PTP
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16712-16719
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
with
Members of the Armadillo Family
(Jiang,
Y.-P., Wang, H., D'Eustachio, P., Musacchio, J. M., Schlessinger, J.,
and Sap, J. (1993) Mol. Cell. Biol. 13, 2942-2951) and was
therefore termed hPTP
. We show here that hPTP
expression is
dependent on cell density and find it colocalized with two members of
the arm family of proteins,
-catenin and
-catenin/plakoglobin, at adherens junctions. Using both in
vitro and in vivo binding assays, we demonstrate
specific complex formation between endogenous hPTP
and
- and
-catenin/plakoglobin. In addition, we present evidence that suggests
that
-catenin may represent a substrate for the catalytic
activity of hPTP
. The identification of specific binding partners
for this receptor-like PTP provides insight into the mechanisms of its
biological action and suggests a role for hPTP
in the regulation of
processes involving cell contact and adhesion such as growth control,
tumor invasion, and metastasis.
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