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Originally published In Press as doi:10.1074/jbc.M106121200 on September 6, 2001

J. Biol. Chem., Vol. 276, Issue 47, 44037-44043, November 23, 2001
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Distinct Regions of the Cadherin Cytoplasmic Domain Are Essential for Functional Interaction with Galpha 12 and beta -Catenin*

Daniel D. KaplanDagger §, Thomas E. MeigsDagger , and Patrick J. CaseyDagger ||

From the Departments of Dagger  Pharmacology and Cancer Biology and  Biochemistry, Duke University Medical Center, Durham, North Carolina 27710

Heterotrimeric G proteins of the G12 subfamily mediate cellular signals leading to events such as cytoskeletal rearrangements, cell proliferation, and oncogenic transformation. Several recent studies have revealed direct effector proteins through which G12 subfamily members may transmit signals leading to various cellular responses. Our laboratory recently demonstrated that Galpha 12 and Galpha 13 specifically interact with the cytoplasmic domains of several members of the cadherin family of cell adhesion molecules (Meigs, T. E., Fields, T. A., McKee, D. D., and Casey, P. J. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 519-524). This interaction causes beta -catenin to release from cadherin and relocalize to the cytoplasm and nucleus, where it participates in transcriptional activation. Here we report that two distinct regions of the epithelial cadherin (E-cadherin) tail are required for interaction with beta -catenin and Galpha 12, respectively. Deletion of an acidic, 19-amino acid region of E-cadherin abolishes its ability to bind beta -catenin in vitro, to inhibit beta -catenin-mediated transactivation, or to stabilize beta -catenin; causes subcellular mislocalization of beta -catenin; and disrupts cadherin-mediated cell adhesion. On the other hand, deletion of a distinct 11-amino acid region of E-cadherin dramatically attenuates interaction with Galpha 12; furthermore, Galpha 12 is ineffective in stimulating beta -catenin release from an E-cadherin cytoplasmic domain lacking this putative Galpha 12-binding region. These findings indicate that Galpha 12 and beta -catenin do not compete for the same binding site on cadherin and provide molecular targets for selectively disrupting the interaction of these proteins with cadherin.

* This work was supported in part by National Institutes of Health Grants GM55717 (to P. J. C.) and CA91159 (to P. J. C. and T. E. M.).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.

§ A Howard Hughes Medical Institute Predoctoral Fellow.

|| To whom correspondence should be addressed: Dept. of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710-3813. Tel.: 919-613-8613; Fax: 919-613-8642; E-mail: casey006@mc.duke.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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