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Article (Scientific journals)
The oncoprotein Bcl-3 can facilitate NF-kappa B-mediated transactivation by removing inhibiting p50 homodimers from select kappa B sites.
Franzoso, G.; Bours, Vincent; Azarenko, V. et al.
1993In EMBO Journal, 12 (10), p. 3893-901
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Keywords :
Animals; Ankyrins/metabolism; Binding Sites; Cell Nucleus/metabolism; DNA/metabolism; Fluorescent Antibody Technique; NF-kappa B/metabolism; Proto-Oncogene Proteins/metabolism; Repetitive Sequences, Nucleic Acid; Transcription Factors; Transcriptional Activation; Tumor Cells, Cultured
Abstract :
[en] Previously we have proposed a role for Bcl-3 in facilitating transactivation through kappa B sites by counteracting the inhibitory effects of bound, non-transactivating homodimers of the p50 subunit of NF-kappa B. Such homodimers are abundant for example in nuclei of unstimulated primary T cells. Here we extend the model and provide new evidence which fulfills a number of predictions. (i) Bcl-3 preferentially targets p50 homodimers over NF-kappa B heterodimers since the homodimers are completely dissociated from kappa B sites at concentrations of Bcl-3 which do not affect NF-kappa B. (ii) Select kappa B sites associate very strongly and stably with p50 homodimers, completely preventing binding by NF-kappa B. Such kappa B sites are likely candidates for regulation by p50 homodimers and Bcl-3. (iii) Bcl-3 and p50 can be co-localized in the nucleus, a requirement for active removal of homodimers from their binding sites in vivo. (iv) The ankyrin repeat domain of Bcl-3 is sufficient for the reversal of p50 homodimer-mediated inhibition, correlating with the ability of this domain alone to inhibit p50 binding to kappa B sites in vitro. Our data support the model that induction of nuclear Bcl-3 may be required during cellular stimulation to actively remove stably bound p50 homodimers from certain kappa B sites in order to allow transactivating NF-kappa B complexes to engage. This exact mechanism is demonstrated with in vitro experiments.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Franzoso, G.
Bours, Vincent ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > GIGA-R : Génétique humaine
Azarenko, V.
Park, S.
Tomita-Yamaguchi, M.
Kanno, T.
Brown, K.
Siebenlist, U.
Language :
English
Title :
The oncoprotein Bcl-3 can facilitate NF-kappa B-mediated transactivation by removing inhibiting p50 homodimers from select kappa B sites.
Publication date :
1993
Journal title :
EMBO Journal
ISSN :
0261-4189
eISSN :
1460-2075
Publisher :
Oxford University Press, Oxford, United Kingdom
Volume :
12
Issue :
10
Pages :
3893-901
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 23 November 2010

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