Cited by 321Estrogen and related hormone effectsReceptor Mechanisms and SignalingAdrenal Hormones and Disorders

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Deciphering the Phosphorylation “Code” of the Glucocorticoid Receptor in Vivo

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Wang, Zhen, Frederick, Jeremy, Garabedian, Michael J.·2002·Journal of Biological Chemistry

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Abstract

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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Authors: Wang, Z., Frederick, J., & Garabedian, M. J.
Affiliations: New York University (US)
Corresponding author: Garabedian, Michael J.
ORCID: Wang, Zhen
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)
DOI: 10.1074/jbc.m110530200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6689 d)
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 › Endocrinology › 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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Deciphering the Phosphorylation “Code” of the Glucocorticoid Receptor in Vivo

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