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See detailThe repressing function of the oncoprotein BCL-3 requires CtBP while its polyubiquitination and degradation involve the E3 ligase TBLR1
Keutgens, Aurore ULg; Shostak, Kateryna ULg; Close, Pierre ULg et al

in Molecular & Cellular Biology (2010), 30

The nuclear and oncogenic BCL-3 protein activates or represses gene transcription when bound to NF-kB proteins p50 and p52, yet the molecules that specifically interact with BCL-3 and drive BCL-3-mediated ... [more ▼]

The nuclear and oncogenic BCL-3 protein activates or represses gene transcription when bound to NF-kB proteins p50 and p52, yet the molecules that specifically interact with BCL-3 and drive BCL-3-mediated effects on gene expression remain largely uncharacterized. Moreover, GSK3-mediated phosphorylation of BCL-3 triggers its degradation through the proteasome, but the proteins involved in this degradative pathway are poorly characterized. Biochemical purification of interacting partners of BCL-3 led to the identification of CtBP as a molecule required for the ability of BCL-3 to repress gene transcription. CtBP is also required for the oncogenic potential of BCL-3 and for its ability to inhibit UV-mediated cell apoptosis in keratinocytes. We also defined the E3 ligase TBLR1 as a protein involved in BCL-3 degradation through a GSK3-independent pathway. Thus, our data demonstrate that the LSD1/CtBP complex is required for the repressing abilities of an oncogenic IkB protein, and they establish a functional link between the E3 ligase TBLR1 and NF-kB. [less ▲]

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