NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2.
Nuclear factor kappaB (NF-kappaB) is a transcription factor that controls the expression of many cellular and viral genes. The p65 (RelA) subunit plays a critical role as a transcriptional activator and 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 by pull-down assay in vitro and by a mammalian two-hybrid assay in vivo. We observed that full-length 53BP2 fused to GFP had a punctate distribution in cytoplasm, predominantly in perinuclear region whereas the N-terminal 53BP2 localized in cytoplasm and C-terminal 53BP2 localized in the nucleus. Furthermore, we found that overexpression of GFP-53BP2 induced apoptosis in transiently transfected cells. Neither the N-terminal nor the C-terminal of 53BP2 fused to GFP induced cell death. Interestingly, co-transfection with a p65 expression plasmid significantly inhibited 53BP2-induced cell death. The previous findings that 53BP2 bound to p53 and Bcl-2 together with our present observations suggest that 53BP2 may play a central role in the regulation of apoptosis and cell growth.
Mesh Terms:
Animals, Ankyrins, Apoptosis, Apoptosis Regulatory Proteins, COS Cells, Carrier Proteins, Cell Cycle, Cell Line, Transformed, Cercopithecus aethiops, HeLa Cells, Humans, NF-kappa B, Protein Binding, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Saccharomyces cerevisiae, Transcription Factor RelA, src Homology Domains
Animals, Ankyrins, Apoptosis, Apoptosis Regulatory Proteins, COS Cells, Carrier Proteins, Cell Cycle, Cell Line, Transformed, Cercopithecus aethiops, HeLa Cells, Humans, NF-kappa B, Protein Binding, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Saccharomyces cerevisiae, Transcription Factor RelA, src Homology Domains
Oncogene
Date: Sep. 16, 1999
PubMed ID: 10498867
View in: Pubmed Google Scholar
Download Curated Data For This Publication
214784
Switch View:
- Interactions 7