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NF-κB p65サブユニットは53BP2と結合し、53BP2によるアポトーシスを抑制する：楊建平、堀真由美、河邊拓己、岡本尚（名市大・分子医学研．分子遺伝）
NF-kB subunit p65 binds to 53BP2 and inhibits 53BP2-induced apoptosis : Jina-Ping YANG, Mayumi HORI, Takumi KAWABE and Takashi OKAMOTO (Dept. Mol. Genetics, Nagoya City Univ.)

Nuclear factor κB (NF-κB) is a transcription factor that controls the expression of many cellular and viral genes. In particular, the p65 (RelA) subunit plays a critical role as a transcriptional activator. Recent observations have highlighted its role in the control of apoptosis. Here we report that 53BP2, a protein previously identified by interaction with wild type p53 and Bcl-2, also binds to p65 in a yeast two-hybrid system. This specific interaction was confirmed in a mammalian two-hybrid system. An in vitro binding assay using recombinant proteins showed that either the ankyrin repeats or the SH3 domain of 53BP2 can interact with p65. We found that overexpression of 53BP2 induced apoptosis in transiently transfected cells. Truncated 53BP2 mutants lacking the p65-interacting domain did not induce apoptosis. Interestingly, co-transfection with a p65 expression plasmid significantly inhibited 53BP2-induced apoptosis. The findings that 53BP2 binds to p53 and Bcl-2 together with these observations suggest that 53BP2 has an central role in the regulation of apoptosis.