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The candidate oncoprotein Bcl-3 is an antagonist of pSO/NF-κB-mediated inhibition

NaturePublished 1 September 1992
Guido Franzoso, Vincent Bours, Sun Park, Michiyo Tomfta-Yamaguchi, Kathleen Kelly, Ulrich Siebenlist
Citations322
SJR quartileQ1
SJR score18.29
SNIP10.16

TL;DR

It is demonstrated that Bcl-3 can aid κB site-dependent transcription in vivo by counteracting the inhibitory effects of p50/NF-κB homodimers, and may therefore aid activation of select NF-κBs-regulated genes, including those of the human immunodeficiency virus.

Abstract

The candidate oncogene bcl-3 was discovered as a translocation into the immunoglobulin alpha-locus in some cases of B-cell chronic lymphocytic leukaemias. The protein Bcl-3 contains seven so-called ankyrin repeats. Similar repeat motifs are found in a number of diverse regulatory proteins but the motifs of Bcl-3 are most closely related to those found in I kappa B proteins in which the ankyrin repeat domain is thought to be directly involved in inhibition of NF-kappa B activity. No biological function has yet been described for Bcl-3, but it was noted recently that Bcl-3 interferes with DNA-binding of the p50 subunit of NF-kappa B in vitro. Here we demonstrate that Bcl-3 can aid kappa B site-dependent transcription in vivo by counteracting the inhibitory effects of p50/NF-kappa B homodimers. Bcl-3 may therefore aid activation of select NF-kappa B-regulated genes, including those of the human immunodeficiency virus.

Keywords

MedicineBiochemistry, Genetics and Molecular Biology