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Originally published In Press as doi:10.1074/jbc.C000639200 on September 27, 2000

J. Biol. Chem., Vol. 275, Issue 46, 35680-35683, November 17, 2000
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ACCELERATED PUBLICATION
A Positive Role for the PP2A Catalytic Subunit in Wnt Signal Transduction*

Marianne J. RatcliffeDagger , Keiji Itoh, and Sergei Y. Sokol

From the Department of Microbiology and Molecular Genetics, Harvard Medical School, Molecular Medicine Unit, Beth Israel Deaconess Medical Center, Boston, Massachessetts 02215

Protein phosphatase-2A (PP2A) is a multisubunit serine/threonine phosphatase involved in intracellular signaling, gene regulation, and cell cycle progression. Different subunits of PP2A bind to Axin and Adenomatous Polyposis Coli, components of the Wnt signal transduction pathway. Using early Xenopus embryos, we studied how PP2A functions in Wnt signal transduction. The catalytic subunit of PP2A (PP2A-C) potentiated secondary axis induction and Siamois reporter gene activation by Dishevelled, a component of the Wnt pathway, indicating a positive regulatory role of this enzyme in Wnt signaling. In contrast, small t antigen, an antagonist of PP2A-C, inhibited Dishevelled-mediated signal transduction, as did the regulatory PP2A-B'epsilon subunit, consistent with the requirement of PP2A function in this pathway. Although Wnt signaling is thought to occur via regulation of beta -catenin degradation, PP2A-C did not significantly affect beta -catenin stability. Moreover, the pathway activated by a stabilized form of beta -catenin was sensitive to PP2A-C and its inhibitors, suggesting that PP2A-C acts downstream of beta -catenin. Because previous work has suggested that PP2A can act upstream of beta -catenin, we propose that PP2A regulates the Wnt pathway at multiple levels.

* This work was supported by National Institutes of Health grants (to S. Y. 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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF298157.

Dagger To whom correspondence should be addressed: Dept. of Microbiology and Molecular Genetics, Harvard Medical School, Molecular Medicine Unit, RW 663, Beth Israel Deaconess Medical Center, East Campus, 330 Brookline Ave., Boston, MA 02215. Tel.: 617-667-3746; Fax: 617-667-2913; E-mail: mratclif@caregroup.harvard.edu.

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