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J Biol Chem, Vol. 275, Issue 4, 2399-2403, January 28, 2000

Protein Phosphatase 2Calpha Dephosphorylates Axin and Activates LEF-1-dependent Transcription*

Erin T. Strovel, Dianqing WuDagger , and Daniel J. Sussman§

From the Division of Human Genetics, University of Maryland School of Medicine, Baltimore, Maryland 21201 and the Dagger  Department of Pharmacology and Physiology, University of Rochester, Rochester, New York 14642

The Dishevelled (Dvl) gene family encodes cytoplasmic proteins that are necessary for Wnt signal transduction. Utilizing the yeast two-hybrid system, we identified protein phosphatase 2Calpha (PP2C) as a Dvl-PDZ domain-interacting protein. PP2C exists in a complex with Dvl, beta -catenin, and Axin, a negative regulator of Wnt signaling. In a Wnt-responsive LEF-1 reporter gene assay, expression of PP2C activates transcription and also elicits a synergistic response with beta -catenin and Wnt-1. In addition, PP2C expression relieves Axin-mediated repression of LEF-1-dependent transcription. PP2C utilizes Axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that PP2C is a positive regulator of Wnt signal transduction and mediates its effects through the dephosphorylation of Axin.

* This work was supported by NCI, National Institutes of Health, Grant RO1 CA63929 (to D. J. S.).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: Div. of Human Genetics, University of Maryland School of Medicine, 655 W. Baltimore St., Baltimore, MD 21201. Tel.: 410-706-8497; Fax: 410-706-6105, E-mail: dsussman@ummc001.ummc.umaryland.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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