Phosphorylation of the Retinoid X Receptor at the Omega loop, modulates the expression of retinoic-acid-target genes with a promoter context specificity
Abstract
The retinoid response is mediated by two classes of nuclear receptors, the retinoic acid receptors (RARalpha, beta, and gamma) and the retinoid X receptors (RXRalpha, beta, and gamma) which act as ligand-dependent heterodimeric RAR/RXR transcription activators. Like most transcription factors, RARs and RXRs are regulated by phosphorylation processes. Here, we report that stress agents induce RXRalpha phosphorylation, subsequently to the activation of the stress-activated protein kinases cascade (JNKs). This phosphorylation process concerns three residues located in the N-terminal AF-1 domain of RXRalpha and one located in the omega loop of the Ligand Binding Domain. To decipher how stress-induced RXRalpha phosphorylation influences the transcription of RA-target genes, we used a ribotoxic stress agent, anisomycin, which activates signaling kinases without promoting DNA or protein damages, at subinhibitory concentrations. Taking advantage of vectors expressing recombinant RXRalpha mutated at its phosphorylation sites and of F9 cell lines re-expressing the same RXRalpha mutants in an RXRalpha null background, we provide evidence that stress signaling modulates RAR/RXRalpha-mediated transcription, through the phosphorylation of RXRalpha at the residue located in the Omega loop, in a promoter context-dependent manner.
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p38MAPK phosphorylates RXRα at three residues located in the NTD.
“Indeed, p38MAPK phosphorylates RXR ␣ at three residues located in the NTD ( 144, 145 ), but the consequences on transcription remain ill defi ned.”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [144]
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Rose is a rose is a rose. Especially if you're a George
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Role of endogenous IGFBP-3 in mammary epithelial cell apoptosis
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RXR – centralny regulator wielu ścieżek sygnałowych w organizmie
Sołtys, K., Leszczyński, B., & Ożyhar, A. (2021) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.2478/ahem-2021-0005
- Authors
- Bruck, N., Bastien, J., Bour, G., Tarrade, A., Plassat, J.-L., Bauer, A., Adam-Stitah, S., & Rochette-Egly, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Venue
- Cellular Signalling
- Publisher
- Elsevier BV
- Published
- 2005-10
- Volume
- 17
- Issue
- 10
- Pages
- 1229-1239
- ISSN
- 0898-6568 (ISSN-L)
- OpenAlex
- W1974892121
- Cited by
- 52
- References
- 55
- Citations by year
- 2026: 2 · 2024: 1 · 2022: 1 · 2021: 1 · 2019: 3 · 2017: 1 · 2016: 2 · 2015: 4 · 2014: 6 · 2013: 1
- FWCI
- 2.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cellular Signalling (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Bristol-Myers Squibb
- Association pour la Recherche sur le Cancer
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- 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 › Peroxisome Proliferator-Activated Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- retinoid X receptor alpha, omega loop, ligand-binding domain, retinoic acid receptor, RAR/RXR heterodimers, c-Jun N-terminal kinase, JNK, anisomycin, ribotoxic stress, transcriptional regulation
- MeSH terms
- Retinoic Acid Receptor alpha, Retinoic Acid 4-Hydroxylase, Retinoic Acid Receptor gamma, Homeobox A1 Protein, Animals, Anisomycin, Chlorocebus aethiops, Cytochrome P-450 Enzyme System, Gene Expression Regulation, Mutation, Phosphorylation, Promoter Regions, Genetic, Serine, Transcription Factors, Transfection, Tretinoin, Signal Transduction, Gene Expression, Receptors, Retinoic Acid, Homeodomain Proteins, COS Cells, Cell Line, Tumor, Retinoid X Receptor alpha, JNK Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, Mice
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