Binding of APC to the Human Homolog of the Drosophila Discs Large Tumor Suppressor Protein
- 17 May 1996
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 272 (5264), 1020-1023
- https://doi.org/10.1126/science.272.5264.1020
Abstract
The adenomatous polyposis coli gene (APC) is mutated in familial adenomatous polyposis and in sporadic colorectal tumors, and its product binds to the adherens junction protein β-catenin. Overexpression of APC blocks cell cycle progression. The APC-β-catenin complex was shown to bind to DLG, the human homolog of the Drosophila discs large tumor suppressor protein. This interaction required the carboxyl-terminal region of APC and the DLG homology repeat region of DLG. APC colocalized with DLG at the lateral cytoplasm in rat colon epithelial cells and at the synapse in cultured hippocampal neurons. These results suggest that the APC-DLG complex may participate in regulation of both cell cycle progression and neuronal function.Keywords
This publication has 29 references indexed in Scilit:
- Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinasesNature, 1995
- The multistep nature of cancerTrends in Genetics, 1993
- APC mutations occur early during colorectal tumorigenesisNature, 1992
- Somatic mutations of the APC gene in colorectal tumors: mutation cluster region in the APC geneHuman Molecular Genetics, 1992
- Identification of FAP Locus Genes from Chromosome 5q21Science, 1991
- Identification and characterization of the familial adenomatous polyposis coli geneCell, 1991
- The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctionsCell, 1991
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue.The Journal of cell biology, 1981
- Use of colloidal gold particles in double-labeling immunoelectron microscopy of ultrathin frozen tissue sections.The Journal of cell biology, 1981