TFIIH Interacts with the Retinoic Acid Receptor γ and Phosphorylates Its AF-1-activating Domain through cdk7
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Retinoic acid receptor gamma (RARgamma) is phosphorylated in COS-1 cells at two conserved serine residues located in the N-terminal region (serines 77 and 79 in RARgamma1 and serines 66 and 68 in RARgamma2) that contains the activation function AF-1. These serines are phosphorylated in vitro by cdk7, a cyclin-dependent kinase associated to cyclin H and MAT1 in the CAK complex (cdk7.cyclin H. MAT1), that is found either free or as a component of the transcription/DNA repair factor TFIIH. RARgamma is more efficiently phosphorylated by TFIIH than by CAK and interacts not only with cdk7 but also with several additional subunits of TFIIH. RARgamma phosphorylation and interaction with TFIIH occur in a ligand-independent manner. Our data demonstrate also that phosphorylation of the AF-1 function modulates RARgamma transcriptional activity in a response gene-dependent manner.
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The RARγ subtype is also phosphorylated at the LBD and at the NTD.
“The RAR ␥ subtype is also phosphorylated at the LBD and at the NTD ( 131, 133 ), but whether it results from the same cascade as above is under investigation.”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [133]
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- Authors
- Bastien, J., Adam-Stitah, S., Riedl, T., Egly, J.-M., Chambon, P., & Rochette-Egly, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Egly, Jean-Marc
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 275
- Issue
- 29
- Pages
- 21896-21904
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038006194
- Cited by
- 107
- References
- 6
- Citations by year
- 2026: 1 · 2024: 2 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 5 · 2013: 3 · 2012: 2
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Bristol-Myers Squibb
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Allergan
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- retinoic acid receptor gamma, TFIIH, CDK7, protein phosphorylation, transcriptional activation, ligand-independent receptor activity, cyclin-dependent kinases, transcriptional regulation
- MeSH terms
- Cyclin-Dependent Kinase-Activating Kinase, Retinoic Acid Receptor gamma, Animals, Humans, Phosphorylation, Transcription Factors, Signal Transduction, Transcriptional Activation, Protein Serine-Threonine Kinases, Receptors, Retinoic Acid, Cyclin-Dependent Kinases, Transcription Factors, TFII, COS Cells, Mice, Transcription Factor TFIIH
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