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Trends Cell Biol. 2007 Jun;17(6):302-9. Epub 2007 Apr 30.

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

Author information

1
Institut de Génétique et de Biologie Moléculaire et Cellulaire, Department of Cell Biology and Signal Transduction, BP10142/Inserm, U596/CNRS, UMR7104, Illkirch, France.

Abstract

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.

PMID:
17467991
DOI:
10.1016/j.tcb.2007.04.003
[Indexed for MEDLINE]

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