APCL, a Central Nervous System-specific Homologue of Adenomatous Polyposis Coli Tumor Suppressor, Binds to p53-binding Protein 2 and Translocates it to the Perinucleus
2000
APCL, a central nervous system-specific sequence homologue of the
adenomatous polyposis coli tumor suppressor, can regulate the
cytoplasmic level of β-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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