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APCL, a Central Nervous System-specific Homologue of Adenomatous Polyposis Coli Tumor Suppressor, Binds to p53-binding Protein 2 and Translocates it to the Perinucleus¹

Division of Clinical Genetics, Biomedical Research Center [H. N., K. K., Y. N.] and the Second Department of Surgery [H. N., M. M.], Osaka University Medical School, Osaka, Japan; Department of Oncogene Research, Institute of Microbial Disease, Osaka University, Osaka, Japan [Y. M., T. A.]; Department of Human Genome Analysis, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research [K. K.] and Laboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan [K. K., Y. N.]

APCL, a central nervous system-specific sequence homologue of the adenomatous polyposis coli tumor suppressor, can regulate the cytoplasmic level of ß-catenin as the adenomatous polyposis coli tumor suppressor does, but its overall biological function remains unclear. Using a yeast two-hybrid system, we attempted to isolate proteins that might associate with the unique COOH-terminus of APCL. Among 166 cDNA clones isolated from a human fetal-brain cDNA library as candidates for interaction with APCL, 32 encoded parts of p53-binding protein 2 (53BP2), a molecule that interacts with p53 and Bcl2. An in vitro binding assay indicated that the Src-homology-3 domain and the ankyrin-repeat domain of 53BP2 were both required for binding to the COOH-terminus of APCL. Confocal microscopy showed that APCL and 53BP2 proteins were localized together in the perinuclei of normal mammalian cells, but this was not the case in cells that expressed truncated APCL and 53BP2 proteins. These findings suggested that binding of the COOH-terminus of APCL to 53BP2 regulates the cytoplasmic location of 53BP2. Because 53BP2 also interacts with p53 and Bcl2 and regulates p53 function, our results suggest that APCL might be involved in the p53/Bcl2-linked pathway of cell-cycle progression and cell death.

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