Abstract
Galectin-3 (gal-3), a member of the beta-galactoside-binding proteins family, was identified as a binding partner of beta-catenin. Analysis of the human gal-3 sequence reveled a structural similarity to beta-catenin as it also contains the consensus sequence (S92XXXS96) for glycogen synthase kinase-3beta (GSK-3beta) phosphorylation and can serve as its substrate. In addition, Axin, a regulator protein of Wnt that complexes with beta-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/beta-catenin signaling pathway and highlight the functional similarities between gal-3 and beta-catenin.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Axin Protein
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Breast Neoplasms / genetics
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Breast Neoplasms / metabolism
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Cell Line, Tumor
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Cytoskeletal Proteins / metabolism
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Galectin 3 / genetics
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Galectin 3 / metabolism*
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Glycogen Synthase Kinase 3 / metabolism
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Glycogen Synthase Kinase 3 beta
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Humans
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Intercellular Signaling Peptides and Proteins / metabolism*
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Phosphorylation
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Protein Binding
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Rats
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Repressor Proteins / metabolism
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Signal Transduction / physiology
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Trans-Activators / metabolism
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Transfection
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Wnt Proteins
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beta Catenin
Substances
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Axin Protein
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CTNNB1 protein, human
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Ctnnb1 protein, rat
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Cytoskeletal Proteins
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Galectin 3
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Intercellular Signaling Peptides and Proteins
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Repressor Proteins
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Trans-Activators
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Wnt Proteins
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beta Catenin
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GSK3B protein, human
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Glycogen Synthase Kinase 3 beta
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Gsk3b protein, rat
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Glycogen Synthase Kinase 3