Abstract
Adenomatous polyposis coli (APC) is an important tumour suppressor in the intestinal epithelium. Its function in reducing nuclear beta-catenin and T-cell factor (TCF)-mediated transcription is conserved from Drosophila to mammals. But APC proteins are also associated with the plasma membrane. Here, we show that mutational inactivation of Drosophila E-APC causes delocalization of Armadillo (the Drosophila beta-catenin) but not DE-cadherin from adhesive plasma membranes. Extensive gaps between these membranes are visible at the ultrastructural level. The oocyte is also mislocalized in E-APC mutant egg chambers, a phenotype that results from a failure of cadherin-based adhesion. These results indicate that Drosophila APC functions in cellular adhesion; these results could have implications for colorectal adenoma formation and tumour progression in humans.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenomatous Polyposis Coli / etiology
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Adenomatous Polyposis Coli / genetics
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Adenomatous Polyposis Coli Protein / genetics
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Adenomatous Polyposis Coli Protein / physiology
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Amino Acid Sequence
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Animals
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Armadillo Domain Proteins
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Cadherins / metabolism
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Cell Adhesion / genetics*
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Drosophila / cytology
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Drosophila / embryology
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Drosophila / genetics*
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Drosophila / metabolism
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Drosophila Proteins / genetics
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Drosophila Proteins / physiology
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Female
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Genes, APC*
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Genes, Insect*
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Humans
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Insect Proteins / metabolism
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Molecular Sequence Data
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Oocytes / cytology
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Phenotype
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Point Mutation
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Sequence Homology, Amino Acid
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Trans-Activators*
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Transcription Factors
Substances
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ARM protein, Drosophila
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Adenomatous Polyposis Coli Protein
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Armadillo Domain Proteins
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Cadherins
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Drosophila Proteins
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Insect Proteins
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Trans-Activators
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Transcription Factors