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J. Biol. Chem., Vol. 277, Issue 12, 10512-10522, March 22, 2002
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From the Plakophilins are a subfamily of
p120-related arm-repeat proteins that can be found in both desmosomes
and the nucleus. Among the three known plakophilin members, plakophilin
1 has been linked to a genetic skin disorder and shown to play
important roles in desmosome assembly and organization. However, little
is known about the binding partners and functions of the most widely
expressed member, plakophilin 2. To better understand the cellular
functions of plakophilin 2, we have examined its protein interactions
with other junctional molecules using co-immunoprecipitation and yeast two-hybrid assays. Here we show that plakophilin 2 can interact directly with several desmosomal components, including desmoplakin, plakoglobin, desmoglein 1 and 2, and desmocollin 1a and 2a. The head
domain of plakophilin 2 is critical for most of these interactions and
is sufficient to direct plakophilin 2 to cell borders. In addition,
plakophilin 2 is less efficient than plakophilin 1 in localizing to the
nucleus and enhancing the recruitment of excess desmoplakin to cell
borders in transiently transfected COS cells. Furthermore, plakophilin
2 is able to associate with
Protein Binding and Functional Characterization of Plakophilin
2
EVIDENCE FOR ITS DIVERSE ROLES IN DESMOSOMES AND 
-CATENIN
SIGNALING*
,
Departments of Pathology and
Dermatology and the Robert H. Lurie Cancer Center, Northwestern
University Medical School, Chicago, Illinois 60611, the
§ Molecular Cell Biology Unit, Department of Molecular
Biology, VIB-University of Ghent, Ledeganckstraat 35, B-9000 Ghent,
Belgium, and the ¶ Molecular Biology Group of the Medical
Faculty, University of Halle, 06097 Halle/Saale, Germany
-catenin through its head domain, and
the expression of plakophilin 2 in SW480 cells up-regulates the
endogenous -catenin/T cell factor-signaling activity. This
up-regulation by plakophilin 2 is abolished by ectopic expression of
E-cadherin, suggesting that these proteins compete for the same pool of
signaling active -catenin. Our results demonstrate that plakophilin
2 interacts with a broader repertoire of desmosomal components than
plakophilin 1 and provide new insight into the possible roles of
plakophilin 2 in regulating the signaling activity of
-catenin.
*
This work is supported by a R. H. Lurie Baseball Charities
Cancer Fellowship (to X. C.), an Institute for the Promotion of Innovation by Science and Technology-Flanders Fellowship (to
S. B), Deutsche Forschungsgemeinschaft Grant Hal791/3-4 (to M. H.), a
Fund for Scientific Research-Flanders grant (to F. v.-R.), and National Institutes of Health Grants RO1 AR43380, PO1 DE12328 (project
4), and AR41836 (to K. G.).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.
To whom correspondence should be addressed: Dept. of
Pathology, Northwestern University Medical School, 303 East Chicago
Ave., Chicago, IL 60611. Tel.: 312-503-5300; Fax: 312-503-8240;
E-mail: kgreen@northwestern.edu.
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