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Implication of Galectin-3 in Wnt Signaling

¹ Department of Tumor Progression and Metastasis, Karmanos Cancer Institute, Wayne State University, Detroit, Michigan; ² Department of General Surgical Science (Department of Surgery I), Graduate School of Medical Sciences, Gunma University, Gunma, Japan; ³ Department of Otolaryngology and Sensory Organs, Osaka University Graduate School of Medicine, Osaka, Japan; ⁴ Department of Urology, School of Medicine, University of Tokushima, Tokushima, Japan; and ⁵ Department of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan

Requests for reprints: Avraham Raz, Tumor Progression and Metastasis Program, Karmanos Cancer Institute, Wayne State University, 110 East Warren Avenue, Detroit, MI 48201. Phone: 313-833-0715; Fax: 313-831-7518; E-mail: raza{at}kci.wayne.edu.

Galectin-3 (gal-3), a member of the ß-galactoside–binding proteins family, was identified as a binding partner of ß-catenin. Analysis of the human gal-3 sequence reveled a structural similarity to ß-catenin as it also contains the consensus sequence (S₉₂XXXS₉₆) for glycogen synthase kinase-3ß (GSK-3ß) phosphorylation and can serve as its substrate. In addition, Axin, a regulator protein of Wnt that complexes with ß-catenin, also binds gal-3 using the same sequence motif identified here by a deletion mutant analysis. The data presented here give credence to the suggestion that gal-3 is a key regulator in the Wnt/ß-catenin signaling pathway and highlight the functional similarities between gal-3 and ß-catenin.

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