Reference : BCL-3 degradation involves its polyubiquitination through a FBW7-independent pathway ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Human health sciences : Laboratory medicine & medical technology
http://hdl.handle.net/2268/71100
BCL-3 degradation involves its polyubiquitination through a FBW7-independent pathway and its binding to the proteasome subunit PSMB1.
English
Keutgens, Aurore mailto [Université de Liège - ULg > Département de pharmacie > Département de pharmacie >]
Zhang-Shao, Xin [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Shostak, Kateryna mailto [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Robert, Isabelle [> > > >]
Olivier, Sabine mailto [Université de Liège - ULg > > Interface Entreprises-Université >]
Vanderplasschen, Alain mailto [Université de Liège - ULg > > Immunologie et vaccinologie >]
Chapelle, Jean-Paul mailto [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Viatour, Patrick [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Merville, Marie-Paule mailto [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Bex, Françoise [> > > >]
Gothot, André mailto [Centre Hospitalier Universitaire de Liège - CHU > > Hématologie biologique et immuno hématologie >]
Chariot, Alain [Centre Hospitalier Universitaire de Liège - CHU > > Chimie médicale >]
2010
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology
285
33
25831–25840
Yes (verified by ORBi)
International
0021-9258
1083-351X
Baltimore
MD
BCL-3 ; polyubiquitination
[en] NF kappa B ; proteasome
[en] The oncogenic protein BCL-3 activates or represses gene transcription through binding with the NF-kappaB proteins p50 and p52 and is degraded through a phospho- and GSK3-dependent pathway. However, the mechanisms underlying its degradation remain poorly understood. Yeast-two-hybrid analysis led to the identification of the proteasome subunit PSMB1 as a BCL-3-associated protein. The binding of BCL-3 to PSMB1 is required for its degradation through the proteasome. Indeed, PSMB1-depleted cells are defective in degrading polyubiquitinated BCL-3. The N-terminal part of BCL-3 includes lysines 13 and 26 required for the K48-linked polyubiquitination of BCL-3. Moreover, the E3 ligase FBW7 known to polyubiquitinate a variety of substrates phosphorylated by GSK3 is dispensable for BCL-3 degradation. Thus, our data defined an unique motif of BCL-3 that is needed for its recruitment to the proteasome and identified PSMB1 as a key protein required for the proteasome-mediated degradation of a nuclear and oncogenic IkappaB protein.
Giga-Signal Transduction
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS, TELEVIE, FBC
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/71100
also: http://hdl.handle.net/2268/73947 ; http://hdl.handle.net/2268/80295
10.1074/jbc.M110.112128

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