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Papers In Press, published online ahead of print October 20, 2000
J. Biol. Chem, 10.1074/jbc.M007665200
Submitted on August 22, 2000
Revised on October 6, 2000
Accepted on October 20, 2000
Biochemistry, UTHSC, Houston, TX 77030
Corresponding Author: Phillip.B.Carpenter{at}uth.tmc.edu
In a screen designed to discover suppressors of mitotic catastrophe, we identified the Xenopus homologue of 53BP1 (X53BP1), a BRCT protein previously identified in humans through its ability to bind the p53 tumor suppressor. X53BP1 transcripts are highly expressed in ovaries and the protein interacts with Xp53 throughout the cell cycle in embryonic extracts. However, no interaction between X53BP1 and Xp53 can be detected in somatic cells, suggesting that the association between the two proteins may be developmentally regulated. X53BP1 is modified via phosphorylation in a DNA-damage dependent manner that correlates with the dispersal of X53BP1 into multiple foci throughout the nucleus in somatic cells. Thus, X53BP1 can be classified as a novel participant in the DNA damage response pathway. We demonstrate that X53BP1 and its human ortholog can serve as good substrates in vitro as well as in vivo for the ATM kinase. Collectively, our results reveal that 53BP1 plays an important role in the checkpoint response to DNA damage, possibly in collaboration with ATM.
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