Reference : Human RelB (I-Rel) functions as a kappa B site-dependent transactivating member of th...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/76742
Human RelB (I-Rel) functions as a kappa B site-dependent transactivating member of the family of Rel-related proteins.
English
Bours, Vincent mailto [Université de Liège - ULiège > Département des sciences biomédicales et précliniques > GIGA-R : Génétique humaine >]
Azarenko, V. [> > > >]
Dejardin, Emmanuel mailto [Université de Liège - ULiège > > GIGA-R : Virologie - Immunologie >]
Siebenlist, U. [> > > >]
1994
Oncogene
Nature Publishing Group
9
6
1699-702
Yes (verified by ORBi)
International
0950-9232
1476-5594
Basingstoke
United Kingdom
[en] Animals ; Base Sequence ; DNA/metabolism ; Humans ; Mice ; Molecular Sequence Data ; NF-kappa B/metabolism ; Proto-Oncogene Proteins ; Species Specificity ; Trans-Activators/physiology ; Transcription Factor RelB ; Transcription Factors/physiology ; Transfection
[en] RelB belongs to the family of Rel-related proteins, dimers of which determine NF-kappa B activity. The murine RelB protein has been reported to be a dimerizing partner in kappa B-binding complexes which are capable of transactivation. On the other hand, the I-Rel protein, the presumed human homolog of RelB, was proposed to be an inhibitor whose presence in dimeric complexes interfered with their kappa B binding and therefore interfered also with transactivation. We demonstrate that human RelB (I-Rel) forms with p50 and p52 (p50B) kappa B-binding heterodimeric complexes which potently transactivate kappa B-dependent constructs in transfection studies. It is concluded that human RelB (I-Rel) and murine RelB can both function as transactivators and that no significant species-specific differences exist.
http://hdl.handle.net/2268/76742

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