Site-directed mutagenesis of the phosphorylation sites in the mouse glucocorticoid receptor.
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The functional significance of receptor phosphorylation in mediating the actions of glucocorticoids remains undefined. The identification of seven phosphorylation sites in the mouse glucocorticoid receptor (Bodwell, J. E., Orti, E., Coull, J. M., Pappin, D. J. C., Smith, L. I., and Swift, F. (1991) J. Biol. Chem. 266, 7549-7555) permits a direct examination of the potential regulatory role of glucocorticoid receptor phosphorylation in transactivation. Using oligonucleotide-directed mutagenesis of the mouse glucocorticoid receptor cDNA, we have substituted alanine or aspartate for the residues phosphorylated in this ligand-dependent transcription factor. COS-1 cells were cotransfected with mutant receptor cDNA expression vectors and a reporter plasmid containing the glucocorticoid-inducible mouse mammary tumor virus promoter linked to chloramphenicol acetyltransferase in order to characterize the effect of these substitutions on receptor-mediated gene expression. Substitution of alanine or aspartate at single phosphorylation sites does not prevent receptor transactivation. Receptors containing multiple substitutions of alanine or aspartate at the major phosphorylation sites in the acidic domain elicit levels of hormone-induced reporter gene expression that are comparable to wild-type receptors. Mutant receptors substituted with alanine at the five phosphorylation sites conserved among the rat, human, and mouse receptors exhibit a 22% decrease in transcriptional activity. Receptors mutated at all seven sites display a similar modest reduction. These results demonstrate that receptor phosphorylation at these seven identified residues is not a major determinant in glucocorticoid receptor transcriptional activity at the mouse mammary tumor virus promoter.
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Multiple kinases differentially phosphorylate the GR at serine residues S203, S211 and S226, regulating GR nuclear translocation and GR-dependent gene transcription.
“Multiple kinases have been reported to differentially phosphorylate the GR at its serine residues, S203, S211 and S226, an effect which regulates GR nuclear translocation and GR-dependent gene transcription.25, 26, 27, 28, 29”
From Antidepressants increase human hippocampal neurogenesis by activating the glucocorticoid receptor (2011) · cites this paper as [29]
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- Authors
- Mason, S. A., & Housley, P. R.
- Affiliations
- University of South Carolina (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-10
- Volume
- 268
- Issue
- 29
- Pages
- 21501-21504
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1597897944
- Cited by
- 94
- References
- 42
- Citations by year
- 2021: 1 · 2020: 1 · 2019: 2 · 2017: 1 · 2015: 1 · 2013: 1 · 2012: 1
- FWCI
- 6.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk036905-03)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-36905)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- glucocorticoid receptor, receptor phosphorylation, phosphorylation sites, transcriptional activation, transcriptional activity, acidic domain, alanine substitution, aspartate substitution, mouse mammary tumor virus promoter, hormone-induced gene expression, ligand-dependent transcription factors
- MeSH terms
- Animals, Cell Line, Genetic Vectors, Mammary Tumor Virus, Mouse, Phosphorylation, Promoter Regions, Genetic, Receptors, Glucocorticoid, Mutagenesis, Site-Directed, DNA, Complementary, Mice
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