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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-3-4
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
208-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11862214-Adenomatous Polyposis Coli,
pubmed-meshheading:11862214-Adenomatous Polyposis Coli Protein,
pubmed-meshheading:11862214-Amino Acid Sequence,
pubmed-meshheading:11862214-Animals,
pubmed-meshheading:11862214-Armadillo Domain Proteins,
pubmed-meshheading:11862214-Cadherins,
pubmed-meshheading:11862214-Cell Adhesion,
pubmed-meshheading:11862214-Drosophila,
pubmed-meshheading:11862214-Drosophila Proteins,
pubmed-meshheading:11862214-Female,
pubmed-meshheading:11862214-Genes, APC,
pubmed-meshheading:11862214-Genes, Insect,
pubmed-meshheading:11862214-Humans,
pubmed-meshheading:11862214-Insect Proteins,
pubmed-meshheading:11862214-Molecular Sequence Data,
pubmed-meshheading:11862214-Oocytes,
pubmed-meshheading:11862214-Phenotype,
pubmed-meshheading:11862214-Point Mutation,
pubmed-meshheading:11862214-Sequence Homology, Amino Acid,
pubmed-meshheading:11862214-Trans-Activators,
pubmed-meshheading:11862214-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
A Drosophila APC tumour suppressor homologue functions in cellular adhesion.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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