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PMID:10498867

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Citation

Yang, JP, Hori, M, Takahashi, N, Kawabe, T, Kato, H and Okamoto, T (1999) NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2. Oncogene 18:5177-86

Abstract

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.

Links

PubMed Online version:10.1038/sj.onc.1202904

Keywords

Animals; Ankyrins/chemistry; Apoptosis/physiology; Apoptosis Regulatory Proteins; COS Cells; Carrier Proteins/antagonists & inhibitors; Carrier Proteins/genetics; Carrier Proteins/metabolism; Carrier Proteins/physiology; Cell Cycle; Cell Line, Transformed; Cercopithecus aethiops; HeLa Cells; Humans; NF-kappa B/metabolism; NF-kappa B/physiology; Protein Binding; Recombinant Fusion Proteins/metabolism; Repetitive Sequences, Amino Acid; Saccharomyces cerevisiae; Transcription Factor RelA; src Homology Domains

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:NFKB1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete

HUMAN:IKBA

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P19838

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P25963

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13625-2

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q15653

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13625

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete

HUMAN:IKBB

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete

HUMAN:TF65

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete

HUMAN:ASPP2

enables

GO:0051059: NF-kappaB binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete


See also

References

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