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

The Dishevelled (Dvl) gene family encodes cytoplasmic proteins that are necessary forWnt signal transduction. Utilizing the yeast two-hybrid system, we identified protein phosphatase 2Cα (PP2C) as a Dvl-PDZ domain-interacting protein. PP2C exists in a complex with Dvl, β-catenin, and Axin, a negativ...

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Published inThe Journal of biological chemistry Vol. 275; no. 4; pp. 2399 - 2403
Main Authors Strovel, Erin T., Wu, Dianqing, Sussman, Daniel J.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 28.01.2000
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ISSN0021-9258
1083-351X
DOI10.1074/jbc.275.4.2399

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Summary:The Dishevelled (Dvl) gene family encodes cytoplasmic proteins that are necessary forWnt signal transduction. Utilizing the yeast two-hybrid system, we identified protein phosphatase 2Cα (PP2C) as a Dvl-PDZ domain-interacting protein. PP2C exists in a complex with Dvl, β-catenin, and Axin, a negative regulator of Wntsignaling. In a Wnt-responsive LEF-1 reporter gene assay, expression of PP2C activates transcription and also elicits a synergistic response with β-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 andin 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.
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.275.4.2399