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. 1997 Jun 15;16(12):3609–3620. doi: 10.1093/emboj/16.12.3609

Regulation of NFKB1 proteins by the candidate oncoprotein BCL-3: generation of NF-kappaB homodimers from the cytoplasmic pool of p50-p105 and nuclear translocation.

N Watanabe 1, T Iwamura 1, T Shinoda 1, T Fujita 1
PMCID: PMC1169985  PMID: 9218802

Abstract

The candidate oncoprotein BCL-3 has been shown to function as a transcriptional co-activator for homodimers of NF-kappaB p50 and p50B. We expressed BCL-3 ectopically in pro-B cell lines and found that these cells exhibited a dramatic increase in nuclear kappaB motif binding activity of p50 homodimers containing BCL-3 in the complex. Co-transfection and in vitro reconstitution experiments revealed that the complex of p50 with its precursor p105 (p50-p105), which was shown to accumulate in the cytoplasm of the pro-B cell lines, is required for induction of DNA binding of p50 homodimers by BCL-3. However, we could see no in vivo or in vitro evidence of a BCL-3-induced increase in proteolytic processing. Instead, BCL-3-mediated reorganization of NFKB1 subunits was demonstrated in vitro. Immunofluorescence staining clearly demonstrated that the transition from cytoplasmic p50-p105 to nuclear p50 homodimers was induced by BCL-3 expression. Thus BCL-3 has versatile functions: cytoplasmic activation of p50 homodimers, their nuclear translocation and, as previously shown, modulation of the transcriptional machinery in the nucleus.

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