Abstract：
:The oncoprotein BCL-3 is a nuclear transcription factor that activates NF-kappaB target genes through formation of heterocomplexes with p50 or p52. BCL-3 is phosphorylated in vivo, but specific BCL-3 kinases have not been identified so far. In this report, we show that BCL-3 is a substrate for the protein kinase GSK3 and that GSK3-mediated BCL-3 phosphorylation, which is inhibited by Akt activation, targets its degradation through the proteasome pathway. This phosphorylation modulates its association with HDAC1, -3, and -6 and attenuates its oncogenicity by selectively controlling the expression of a subset of newly identified target genes such as SLPI and Cxcl1. Our results therefore suggest that constitutive BCL-3 phosphorylation by GSK3 regulates BCL-3 turnover and transcriptional activity.
journal_name
Mol Celljournal_title
Molecular cellauthors
Viatour P,Dejardin E,Warnier M,Lair F,Claudio E,Bureau F,Marine JC,Merville MP,Maurer U,Green D,Piette J,Siebenlist U,Bours V,Chariot Adoi
10.1016/j.molcel.2004.09.004subject
Has Abstractpub_date
2004-10-08 00:00:00pages
35-45issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(04)00522-2journal_volume
16pub_type
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