Identification of Plakoglobin Domains Required for Association with N-cadherin and 
-Catenin (*)
- ¶To whom correspondence should be addressed: Dept. of Biology, 2801 W. Bancroft St., University of Toledo, Toledo, OH 43606. Tel.: 419-537-4918; Fax: 419-537-7737.
Abstract
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion,
the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three
catenins, α-catenin, β-catenin, and 
-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction
with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that
allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal
deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation
to map the regions of plakoglobin that allow it to associate with N-cadherin and with α-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show that the α-catenin-binding region maps within
the first repeat and the N-cadherin-binding region maps within repeats 7 and 8.
Footnotes
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↵§ These authors contributed equally to this study.
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↵* This work was supported by National Institutes of Health Grant GM51188, by grants from the Ohio Chapters of the American Cancer Society and the American Heart Association, and by the Ohio Board of Regents. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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↵1 The abbreviations used are:
- PCR
-
polymerase chain reaction
- PAGE
-
polyacrylamide gel electrophoresis.
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- Received November 21, 1994.
- Revision received March 22, 1995.
- © 1995 by The American Society for Biochemistry and Molecular Biology, Inc.
