The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Phosphorylation of the retinoic acid receptor-alpha by protein kinase A
Open accessAbstract
The phosphorylation of retinoic acid receptor-alpha 1 (RAR alpha 1) by PKA was investigated both in vitro and in vivo. We show that bacterially expressed RAR alpha 1 is phosphorylated in vitro by protein kinase A (PKA) at the unique serine residue 369 located in the C-terminal end of the E region. We also show that RAR alpha 1 overexpressed in COS-1 cells is phosphorylated on multiple serine residues and that phosphorylation at serine 369 occurs only when COS-1 cells are cotransfected with PKA or treated with forskolin. RAR alpha 1 mutants were constructed in which serine 369 was replaced by an alanine (S369A) or a glutamic acid (S369E) residue. Comparison of the tryptic phosphopeptide patterns of wild type and mutated RAR alpha 1 overexpressed in COS-1 cells allowed us to confirm that serine 369 is the unique phosphorylation site for PKA in cultured cells. The DNA-binding efficiency of RAR alpha/retinoid X receptor-alpha (RXR alpha) heterodimers was enhanced in vitro by the S369E mutation. However, in transfected RAC65 cells, the same S369E mutation did not affect the ligand-dependent transcriptional activation by RAR alpha 1 of reporter genes containing a retinoic acid (RA)-response element. In contrast, the S369A mutation slightly decreased both DNA binding and the efficiency of PKA to enhance RA-induced transactivation by RAR alpha 1. Finally, we show that endogenous RAR alpha is also phosphorylated in vivo at serine 369 in forskolin-treated F9 cells, supporting the idea that phosphorylation of RARs at this site is involved in the modulation of the RA-induced differentiation of F9 cells by (Bu)2cAMP.
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“Studies from our laboratory demonstrated that RARs are phosphorylated at two serine residues, one in the LBD (serine 369 in RAR ␣ ) and the other one in the NTD (serine 77 in RAR ␣ ) ( 130, 131 ) ( Fig. 2A ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [131]
In the citing paper
“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 [131]
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Metadata
- Authors
- Rochette-Egly, C.
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1995-07-01
- Volume
- 9
- Issue
- 7
- Pages
- 860-871
- ISSN
- 0888-8809 (ISSN-L)
- OpenAlex
- W2093523090
- Cited by
- 124
- References
- 46
- Citations by year
- 2024: 1 · 2023: 3 · 2021: 2 · 2019: 2 · 2018: 1 · 2016: 2 · 2015: 4 · 2014: 5 · 2013: 4 · 2012: 3
- FWCI
- 3.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- 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 › Protein Kinase Regulation and GTPase Signaling
- Keywords
- retinoic acid receptor alpha, protein kinase A, phosphorylation sites, forskolin, retinoid X receptor alpha, transcriptional activation, retinoic acid response element, F9 cells, cell differentiation, cyclic AMP
- MeSH terms
- Retinoic Acid Receptor alpha, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, Molecular Sequence Data, Phosphorylation, Protein Kinase C, Transcriptional Activation, Point Mutation, Gene Transfer Techniques, Receptors, Retinoic Acid
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