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Shinya Kobayashi^1,2,, Shinichi Kajino^1,2,, Naoko Takahashi¹, Satoshi Kanazawa¹, Kenichi Imai¹, Yurina Hibi¹, Hirotaka Ohara², Makoto Itoh² and Takashi Okamoto^1,*

¹ Department of Molecular and Cellular Biology, and ² Department of Internal Medicine and Bioregulation, Nagoya City University Graduate School of Medical Sciences, 1 Kawasumi, Mizuho-cho, Mizuho-ku, Nagoya, Aichi 467-8601, Japan

The p53 binding protein 2 (53BP2) has been identified as the interacting protein to p53, Bcl-2, and p65 subunit of nuclear factor B (NF-B). The TP53BP2 gene encodes two splicing variants, 53BP2S and 53BP2L, previously known as apoptosis stimulating protein 2 of p53 (ASPP2). We found that these 53BP2 proteins are located predominantly in the cytoplasm and induce apoptosis as demonstrated by cleavage of poly ADP ribose polymerase (PARP) and annexin V staining. Furthermore, we demonstrate that 53BP2 is located in the mitochondria and induces apoptosis associated with depression of the mitochondrial trans-membrane potential (m) and activation of caspase-9. From these findings we conclude that 53BP2 induces apoptosis through the mitochondrial death pathway.

These two authors contributed equally to this work.

^* Correspondence: E-mail: tokamoto{at}med.nagoya-cu.ac.jp

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