Deciphering the Phosphorylation “Code” of the Glucocorticoid Receptor in Vivo
Open accessAbstract
The glucocorticoid receptor (GR) is phosphorylated at multiple serine residues in a hormone-dependent manner, yet progress on elucidating the function of GR phosphorylation has been hindered by the lack of a simple assay to detect receptor phosphorylation in vivo. We have produced antibodies that specifically recognize phosphorylation sites within human GR at Ser(203) and Ser(211). In the absence of hormone, the level of GR phosphorylation at Ser(211) was low compared with phosphorylation at Ser(203). Phosphorylation of both residues increased upon treatment with the GR agonist dexamethasone. Using a battery of agonists and antagonists, we found that the transcriptional activity of GR correlated with the amount of phosphorylation at Ser(211), suggesting that Ser(211) phosphorylation is a biomarker for activated GR in vivo. Mechanistically, the kinetics of Ser(203) and Ser(211) phosphorylation in response to hormone differed, with Ser(211) displaying a more robust and sustained phosphorylation relative to Ser(203). Analysis of GR immunoprecipitates with phospho-GR-specific antibodies indicated that the receptor was phosphorylated heterogeneously at Ser(203) in the absence of hormone, whereas in the presence of hormone, a subpopulation of receptors was phosphorylated at both Ser(203) and Ser(211). Interestingly, biochemical fractionation studies following hormone treatment indicated that the Ser(203)-phosphorylated form of the receptor was predominantly cytoplasmic, whereas Ser(211)-phosphorylated GR was found in the nucleus. Likewise, by immunofluorescence, Ser(203)-phosphorylated GR was located in the cytoplasm and perinuclear regions of the cell, but not in the nucleoplasm, whereas strong phospho-Ser(211) staining was evident in the nucleoplasm of hormone-treated cells. Our results suggest that differentially phosphorylated receptor species are located in unique subcellular compartments, likely modulating distinct aspects of receptor function.
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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 [25]
Impaired Ser-211 phosphorylation might lead to glucocorticoid resistance in malignant lymphoid cells.
“Impaired Ser-211 phosphorylation might lead to glucocorticoid resistance in malignant lymphoid cells”
From Corticosteroids (2016) · cites this paper as [72]
Ligand-dependent phosphorylation of GR at Ser-211 correlates with elevated transcriptional activity.
“Ligand-dependent phosphorylation of GR at Ser-211 correlates with elevated transcriptional activity, while phosphorylation at Ser-226 decreases GR transcriptional activity.”
From Corticosteroids (2016) · cites this paper as [72]
Phosphorylation of GRα alters its transcriptional activity, often in a gene-specific manner.
“Phosphorylation of GRα changes its transcriptional activity, often in a gene-specific manner71, 72.”
From Corticosteroids (2016) · cites this paper as [72]
Phosphorylation of GR at Ser-226 decreases GR transcriptional activity.
“while phosphorylation at Ser-226 decreases GR transcriptional activity.”
From Corticosteroids (2016) · cites this paper as [72]
Hyperphosphorylation at Ser-226 might account for decreased GR signaling in the pathology of depression.
“hyperphosphorylation at Ser-226 might account for decreased GR signaling in the pathology of depression72, 73.”
From Corticosteroids (2016) · cites this paper as [72]
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- Authors
- Wang, Z., Frederick, J., & Garabedian, M. J.
- Affiliations
- New York University (US)
- Corresponding author
- Garabedian, Michael J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-07
- Volume
- 277
- Issue
- 29
- Pages
- 26573-26580
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2000736584
- Cited by
- 321
- References
- 34
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 14 · 2023: 13 · 2022: 11 · 2021: 11 · 2020: 11 · 2019: 8 · 2018: 12 · 2017: 16 · 2016: 16 · 2015: 12 · 2014: 20 · 2013: 21 · 2012: 18
- FWCI
- 7.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (P30CA016087)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK054836)
- 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
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Keywords
- glucocorticoid receptor, receptor phosphorylation, dexamethasone, transcriptional activity, subcellular localization, cytoplasmic receptors, nuclear receptors
- MeSH terms
- Amino Acid Sequence, Cell Compartmentation, Dexamethasone, Fluocinolone Acetonide, Fluorescent Antibody Technique, Humans, Molecular Sequence Data, Phosphorylation, Prednisolone, Receptors, Glucocorticoid, Serine, Structure-Activity Relationship, Tumor Cells, Cultured, Biomarkers, Transcriptional Activation, Mifepristone, Fluorescent Antibody Technique, Indirect
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