Protein phosphorylation as a key mechanism for the regulation of BCL-3 activity

[en] Constitutive NF-kappaB activation, a hallmark of many human cancers, upregulates anti-apoptotic gene expression and therefore disrupts the balance between apoptosis and proliferation. In some lymphomas, this constitutive NF-kappaB activity is the result of point mutations or translocations of the genes coding for NF-kappaB inhibitors, namely IkappaBalpha or p100. The BCL-3 protein is another member of the IkappaB family and is overexpressed in a subset of human B-cell chronic lymphocytic leukemias because of a chromosomal translocation. This oncoprotein is phosphorylated by multiple kinases including GSK3 and this phosphorylation regulates BCL-3 function by modulating its oncogenic potential and by regulating the expression of a subset of its target genes. Therefore, deciphering the NF-kappaB/IkappaB protein phosphorylations is critical in order to better understand the molecular mechanisms of NF-kappaB-mediated oncogenesis.

Research Center/Unit :

Giga-Signal Transduction - ULiège

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Viatour, Patrick ; Université de Liège - ULiège > Chimie médicale

Merville, Marie-Paule ; Université de Liège - ULiège > Département de pharmacie > Chimie médicale

Bours, Vincent ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Génétique générale et humaine

Chariot, Alain ; Université de Liège - ULiège > Département de pharmacie > Chimie médicale

Language :

English

Title :

Protein phosphorylation as a key mechanism for the regulation of BCL-3 activity

Publication date :

December 2004

Journal title :

Cell Cycle

ISSN :

1538-4101

eISSN :

1551-4005

Publisher :

Landes Bioscience

Volume :

Issue :

Pages :

1498-1501

Peer reviewed :

Peer Reviewed verified by ORBi

Name of the research project :

Insight into the oncogenic potential of BCL-3

Funders :

F.R.S.-FNRS - Fonds de la Recherche Scientifique
Télévie
FBC
ULg. ARC - Université de Liège. Actions de Recherche Concertées

Available on ORBi :

since 26 November 2008

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