The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Dimerization with Retinoid X Receptors and Phosphorylation Modulate the Retinoic Acid-induced Degradation of Retinoic Acid Receptors α and γ through the Ubiquitin-Proteasome Pathway
Open accessAbstract
In eukaryotic cells, the ubiquitin-proteasome pathway is the major mechanism for targeted degradation of proteins. We show that, in F9 cells and in transfected COS-1 cells, the nuclear retinoid receptors, retinoic acid receptor gamma2 (RARgamma2), RARalpha1, and retinoid X receptor alpha1 (RXRalpha1) are degraded in a retinoic acid-dependent manner through the ubiquitin-proteasome pathway. The degradation of RARgamma2 is entirely dependent on its phosphorylation and on its heterodimerization with liganded RXRalpha1. In contrast, RARalpha1 degradation can occur in the absence of heterodimerization, whereas it is inhibited by phosphorylation, and heterodimerization reverses that inhibition. RXRalpha1 degradation is also modulated by heterodimerization. Thus, each partner of RARgamma/RXRalpha and RARalpha/RXRalpha heterodimers modulates the degradation of the other. We conclude that the ligand-dependent degradation of RARs and RXRs by the ubiquitin-proteasome pathway, which is regulated by heterodimerization and by phosphorylation, could be important for the regulation of the magnitude and duration of the effects of retinoid signals.
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“RARs are also degraded by the ubiquitin-proteasome system, through the recruitment of TRIP1/SUG-1, which is a subunit of the 19S regulatory subcomplex of the proteasome with an ATPase activity ( 110-112 ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [110]
In the citing paper
“At the end of the RA signal, the proteasomal degradation of RAR ␥ has been shown to depend on the phosphorylation by p38MAPK of an additional serine residue located in the NTD ( 110, 111 ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [110]
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Self-citation
Metadata
- Authors
- Kopf, E., Plassat, J.-L., Vivat, V., de Thé, H., Chambon, P., & Rochette-Egly, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 275
- Issue
- 43
- Pages
- 33280-33288
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2154503677
- Cited by
- 155
- References
- 68
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 4 · 2020: 2 · 2019: 1 · 2018: 4 · 2017: 4 · 2016: 1 · 2015: 2 · 2014: 6 · 2013: 4 · 2012: 3
- FWCI
- 4.71
- 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
- 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 › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- retinoic acid receptor alpha, retinoic acid receptor gamma, retinoid X receptor alpha, protein degradation, ubiquitin-proteasome system, receptor phosphorylation, heterodimerization, retinoic acid signaling, nuclear receptors
- MeSH terms
- Retinoic Acid Receptor alpha, Retinoic Acid Receptor gamma, Amino Acid Sequence, Animals, Cysteine Endopeptidases, Molecular Sequence Data, Multienzyme Complexes, Phosphorylation, Transcription Factors, Transfection, Tretinoin, Ubiquitins, Receptors, Retinoic Acid, Dimerization, COS Cells, Proteasome Endopeptidase Complex, Retinoid X Receptors
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