Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors.

Gaétan Bour (1) , Sébastien Lalevée (1) , Cécile Rochette-Egly (1)

1 IGBMC - Institut de génétique et biologie moléculaire et cellulaire

Nuclear retinoic acid receptors (RARs) are transcriptional transregulators that control the expression of specific subsets of genes in a ligand-dependent manner. The basic mechanism for switching on gene transcription by agonist-liganded RARs involves their binding at specific response elements located in target genes. It also involves interactions with coregulatory protein complexes, the assembly of which is directed by the C-terminal ligand-binding domain of RARs. In addition to this scenario, several recent studies highlighted a fundamental role for the N-terminal domain in the transcriptional activity of RARs, following phosphorylation by the CDK7 kinase of the general transcription factor TFIIH and by p38MAPK. It has also emerged that the ubiquitin-proteasome system has a key role in RAR-mediated transcription. Here, we review new insights into how N-terminal domain and the proteasome pathway can influence the dynamics of RAR transcriptional activity.

Domaines: Biologie moléculaire

Gaétan Bour, Sébastien Lalevée, Cécile Rochette-Egly. Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors.. Trends in Cell Biology, 2007, 17 (6), pp.302-9. ⟨10.1016/j.tcb.2007.04.003⟩. ⟨hal-00190931⟩