Cited by 124Retinoids in leukemia and cellular processesPeroxisome Proliferator-Activated ReceptorsProtein Kinase Regulation and GTPase Signaling

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Phosphorylation of the retinoic acid receptor-alpha by protein kinase A

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Rochette-Egly, C.·1995·Molecular Endocrinology

DOI 10.1210/me.9.7.860

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Abstract

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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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)
DOI: 10.1210/me.9.7.860
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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Phosphorylation of the retinoic acid receptor-alpha by protein kinase A

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