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J. Biol. Chem., Vol. 276, Issue 18, 14896-14901, May 4, 2001
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From the Department of Molecular Biology and Microbiology, School
of Medicine, Case Western Reserve University,
Cleveland, Ohio 44106-4960
PTPµ, an Ig superfamily receptor
protein-tyrosine phosphatase, promotes cell-cell adhesion and interacts
with the cadherin-catenin complex. The signaling pathway
downstream of PTPµ is unknown; therefore, we used a yeast two-hybrid
screen to identify additional PTPµ interacting proteins. The
membrane-proximal catalytic domain of PTPµ was used as bait.
Sequencing of two positive clones identified the scaffolding protein
RACK1 (receptor for activated protein C kinase) as a PTPµ interacting protein. We
demonstrate that RACK1 interacts with PTPµ when co-expressed in a
recombinant baculovirus expression system. RACK1 is known to bind to
the src protein-tyrosine kinase. This study demonstrates
that PTPµ association with RACK1 is disrupted by the presence of
constituitively active src. RACK1 is thought to be a
scaffolding protein that recruits proteins to the plasma membrane via
an unknown mechanism. We have shown that the association of endogenous
PTPµ and RACK1 in a lung cell line is increased at high cell density.
We also demonstrate that the recruitment of RACK1 to both the plasma
membrane and cell-cell contact sites is dependent upon the presence of
the PTPµ protein in these cells. Therefore, PTPµ may be one of the
proteins that recruits RACK1 to points of cell-cell contact, which may
be important for PTPµ-dependent signaling in response to
cell-cell adhesion.
The PTPµ Protein-tyrosine Phosphatase Binds and Recruits
the Scaffolding Protein RACK1 to Cell-Cell Contacts*
,
*
This work was supported by a grant from the American Cancer
Society, Ohio Division, Cuyahoga County Unit (to S. B. K.)
and by National Institutes of Health Grant 1RO1-EY12251 (to S. B. K.). This work, under DAMD17-98-1-8586, was also supported by the Department of Defense Prostate Cancer Research Program, which is
managed by the U.S. Army Medical Research and Materiel Command. Additional support was provided by Visual Sciences Research Center Core
Grant from National Eye Institute Grant PO-EY11373.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by The Swedish Society for Medical Research.
§
To whom correspondence should be addressed: Dept. of Molecular
Biology and Microbiology, Case Western Reserve University, 10900 Euclid
Ave., Cleveland, OH 44106-4960. Tel.: 216-368-0330; Fax:
216-368-3055; E-mail: smb4@po.cwru.edu.
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