ORBi: Keutgens Aurore - BCL-3 degradation involves its polyubiquitination through a FBW7-independent pathway and its binding to the proteasome subunit PSMB1.

Reference : BCL-3 degradation involves its polyubiquitination through a FBW7-independent pathway and...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology Human health sciences : Laboratory medicine & medical technology
	To cite this reference:	http://hdl.handle.net/2268/71100

Title :	BCL-3 degradation involves its polyubiquitination through a FBW7-independent pathway and its binding to the proteasome subunit PSMB1.
Language :	English
Author, co-author :	Keutgens, Aurore [Université de Liège - ULg > Département de pharmacie > Département de pharmacie >]
	Zhang-Shao, Xin [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
	Shostak, Kateryna [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
	Robert, Isabelle [> > > >]
	Olivier, Sabine [Université de Liège - ULg > > Interface Entreprises-Université >]
	Vanderplasschen, Alain [Université de Liège - ULg > > Immunologie et vaccinologie >]
	Chapelle, Jean-Paul [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
	Viatour, Patrick [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
	Merville, Marie-Paule [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
	Bex, Françoise [> > > >]
	Gothot, André [Centre Hospitalier Universitaire de Liège - CHU > > Hématologie biologique et immuno hématologie >]
	Chariot, Alain [Centre Hospitalier Universitaire de Liège - CHU > > Chimie médicale >]
Publication date :	2010
Journal title :	Journal of Biological Chemistry
Publisher :	American Society for Biochemistry and Molecular Biology
Volume :	285
Issue/season :	33
Pages :	25831–25840
Audience :	International
ISSN :	0021-9258
e-ISSN :	1083-351X
City :	Baltimore
Country :	MD
Keywords :	BCL-3 ; polyubiquitination
	[en] NF kappa B ; proteasome
Abstract :	[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.
Research units :	Giga-Signal Transduction
Funders :	Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS, TELEVIE, FBC
Target :	Researchers ; Professionals ; Students
Permalink :	http://hdl.handle.net/2268/71100
	also: http://hdl.handle.net/2268/73947 ; http://hdl.handle.net/2268/80295
DOI :	10.1074/jbc.M110.112128

File(s) associated to this reference

Fulltext file(s):

	File	Commentary	Version	Size	Access
Open access	BCL 3 degradation involves its polybiquitination ... full text.pdf		Publisher postprint	868.71 kB	View/Open

All documents in ORBi are protected by a user license.

Dspace v1.5