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1 Karmanos Cancer Institute, Wayne State University Medical School, Detroit, Michigan; and 2 Department of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan
Galectin-3 (gal-3), a pleiotrophic protein, is an important regulator of tumor metastasis, which like ß-catenin shuttles between the nucleus and the cytosol in a phosphorylation-dependent manner. We report herein that ß-catenin stimulation of cyclin D1 and c-myc expression is gal-3 dependent. Gal-3 binds to ß-catenin/Tcf complex, colocalizes with ß-catenin in the nucleus, and induces the transcriptional activity of Tcf-4 as determined by the TOP/FOPFLASH reporter system. We have identified the ß-catenin–gal-3–binding sequences, which are in the NH2 and COOH termini of the proteins encompassing amino acid residues 1 to 131 and 143 to 250, respectively. These data indicate that gal-3 is a novel binding partner for ß-catenin involved in the regulation of Wnt/ß-catenin signaling pathway.
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