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

@article{Franzoso1992TheCO,
  title={The candidate oncoprotein Bcl-3 is an antagonist of pSO/NF-$\kappa$B-mediated inhibition},
  author={G. Franzoso and Vincent Bours and Sun Ock Park and Michiyo Tomfta-Yamaguchi and Kathleen Kelly and Ulrich Siebenlist},
  journal={Nature},
  year={1992},
  volume={359},
  pages={339-342}
}
THE candidate oncogene bcl-3 was discovered as a translocation into the immunoglobulin alphalocus in some cases of B-cell chronic lymphocytic leukaemias1. 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 1κB proteins in which the ankyrin repeat domain is thought to be directly involved in inhibition of NF-κB activity. No biological function has… 
The Putative Oncoprotein Bcl-3 Induces Cyclin D1 To Stimulate G1 Transition
TLDR
It is demonstrated that dysregulated expression of Bcl-3 potentiates the G1 transition of the cell cycle by stimulating the transcription of the cyclin D1 gene in human breast epithelial cells.
The Bcl-3 oncoprotein acts as a bridging factor between NF-κB/Rel and nuclear co-regulators
TLDR
Data implicate Bcl-3 as an adaptor between NF-κB p50/p52 and other transcription regulators and suggest that its gene activation function may at least in part be due to recruitment of the Tip60 histone actetylase.
Regulation of Bcl-3 through interaction with the Lck tyrosine kinase.
NF-κB1 (p50) Homodimers Contribute to Transcription of thebcl-2 Oncogene*
TLDR
It is concluded that the p50 homodimer is capable of transcriptional activation of the bcl-2 gene and suggested that its nuclear activity contributes to the expression of Bcl- 2 in LY-ar cells.
The bcl-3 Proto-Oncogene Encodes a Nuclear IidB-Like Molecule That Preferentially Interacts with NF-KB p50 and p52 in a Phosphorylation-Dependent Manner
TLDR
In vitro, Bcl-3 protein specifically inhibited the DNA binding of both the homodimeric NF-KcB p5O subunit and a closely related homolog, p52 (previously p49), to immunoglobulin K NF-cB DNA motifs.
The IκB Protein Bcl-3 Negatively Regulates Transcription of the IL-10 Gene in Macrophages1
TLDR
It is demonstrated that Bcl-3−/− mice are highly susceptible to Listeria monocytogenes infection and this correlates with diminished production of IL-12 p70 and IFN-γ in vivo, which is mainly due to elevated synthesis ofIL-10.
The bcl-3 proto-oncogene encodes a nuclear I kappa B-like molecule that preferentially interacts with NF-kappa B p50 and p52 in a phosphorylation-dependent manner
TLDR
Bcl-3 appears to be a nuclear, I kappa B-related molecule that regulates the activity of homodimeric nuclear p50 and its homolog p52, and partially inactivated its inhibitory properties, implicating a role for phosphorylation in the regulation of B cl-3 activity.
Constitutive expression of Bc1-3 in thymocytes increases the DNA binding of NF-kappaB1 (p50) homodimers in vivo
TLDR
It is shown that Bcl-3 is phosphorylated in thymocytes and that its dephosphorylation greatly decreases the effect on p50 homodimers, and that it is associated with endogenous p50 and p52 in nuclear extracts from transgenic animals.
...
...

References

SHOWING 1-10 OF 35 REFERENCES
Candidate proto-oncogene bcl-3 encodes a subunit-specific inhibitor of transcription factor NF-κB
TLDR
It is shown that the proto-oncogene bcl-3, believed to be involved in certain human B-cell leukaemias17, encodes a protein that functions as an IκB-like molecule for native NF-κB but is specific for the p50 subunit.
The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding.
TLDR
It is shown that the C-terminal half of p105, when expressed as a separate molecule, binds to p50 and can rapidly disrupt protein-DNA complexes of p50 or native NF-kappa B and strongly suggest that the ankyrin repeats in these factors are involved in protein-protein interactions with the rel-like domain of p 50.
Processing of the precursor of NF-κB by the HIV-1 protease during acute infection
TLDR
It is shown here that the HIV-1 protease can process p105 and increases levels of active nuclear NF-κB complex, which is required for efficient transcription1 of the human immunodeficiency virus type-1 genome.
Cloning of an NF-κB subunit which stimulates HIV transcription in synergy with p65
TLDR
P49 acts in synergy with p65 to stimulate the human immunodeficiency virus (HIV) enhancer in transiently transfected Jurkat cells, suggesting p49/plOO NF-κB could be important in the regulation of HIV and other κB-containing genes.
The p65 subunit is responsible for the strong transcription activating potential of NF‐kappa B.
TLDR
The study suggests that the p50 subunit in NF‐kappa B might only serve a helper function in DNA binding whereas the p65 subunit is responsible for initiating transcription.
Rel-associated pp40: an inhibitor of the rel family of transcription factors.
TLDR
The results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.
...
...