TRIM24 mediates the interaction of the retinoic acid receptor alpha with the proteasome
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Updated: Feb 13, 2026
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Published on: December 5, 2016
Marilyn Carrier1, Regis Lutzing1, Samia Gaouar1
1Department of Functional Genomics and Cancer, IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire), INSERM, U964, CNRS, UMR7104, Université de Strasbourg, Illkirch Cedex, France.
Abstract:
The nuclear retinoic acid (RA) receptors (RARα, β and γ) 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 RARα subtype involves ubiquitination and the tripartite motif protein TRIM24, which was originally identified as a ligand-dependent corepressor of RARα. We show that in response to RA, TRIM24 serves as an adapter linking RARα to the proteasome for its degradation. In addition, TRIM24 and the proteasome are recruited with RARα to the promoters of target genes and thus are inherently linked to RARα transcriptional activity.
Insights
The tripartite motif protein TRIM24 links retinoic acid receptor alpha (RARα) to the proteasome for degradation, a process crucial for regulating gene transcription.
Area of Science:
- Molecular Biology
- Gene Regulation
- Protein Degradation
Background:
- Nuclear retinoic acid receptors (RARs) regulate gene transcription upon ligand binding.
- Activated RARs interact with coregulators and are subsequently degraded by the ubiquitin-proteasome system.
Discussion:
- This study reveals TRIM24's novel role in RARα degradation.
- TRIM24 acts as an adapter, connecting RARα to the proteasome for ubiquitination and degradation.
- TRIM24 and the proteasome are recruited to target gene promoters with RARα.
Key Insights:
- TRIM24 is essential for the ubiquitination and proteasomal degradation of RARα.
- TRIM24 functions as a bridge between RARα and the degradation machinery.
- The degradation process is intrinsically linked to RARα's transcriptional activity at target gene promoters.
Outlook:
- Further investigation into TRIM24's role in other RAR subtypes and nuclear receptors.
- Exploring the therapeutic potential of modulating TRIM24-mediated degradation for diseases involving RARα dysregulation.
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