1. <scp>TRIM</scp> 24 mediates the interaction of the retinoic acid receptor alpha with the proteasome
- Author
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Régis Lutzing, Samia Gaouar, Marilyn Carrier, Cécile Rochette-Egly, univOAK, Archive ouverte, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), and Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
0301 basic medicine ,Proteasome Endopeptidase Complex ,Biophysics ,Retinoic acid ,retinoic acid receptor ,Tretinoin ,Biochemistry ,TRIM24 ,03 medical and health sciences ,chemistry.chemical_compound ,Ubiquitin ,Structural Biology ,ubiquitin ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Genetics ,Humans ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Molecular Biology ,degradation ,030102 biochemistry & molecular biology ,biology ,Chemistry ,Retinoic Acid Receptor alpha ,Ubiquitination ,Promoter ,Cell Biology ,Cell biology ,Retinoic acid receptor ,proteasome ,030104 developmental biology ,Proteasome ,Retinoic acid receptor alpha ,Proteolysis ,MCF-7 Cells ,biology.protein ,Carrier Proteins ,transcription ,Corepressor ,HeLa Cells - Abstract
The nuclear retinoic acid (RA) receptors (RARalpha, beta and gamma) are ligand-dependent regulators of transcription. Upon activation by RA, they are recruited at the promoters of target genes together with several coregulators. Then, they are degraded by the ubiquitin proteasome system. Here, we report that the degradation of the RARalpha subtype involves ubiquitination and the tripartite motif protein TRIM24, which was originally identified as a ligand-dependent corepressor of RARalpha. We show that in response to RA, TRIM24 serves as an adapter linking RARalpha to the proteasome for its degradation. In addition, TRIM24 and the proteasome are recruited with RARalpha to the promoters of target genes and thus are inherently linked to RARalpha transcriptional activity.
- Published
- 2018
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