Glucocorticoid Receptor/Signal Transducer and Activator of Transcription 5 (STAT5) Interactions Enhance STAT5 Activation by Prolonging STAT5 DNA Binding and Tyrosine Phosphorylation

Wyszomierski, Shannon L.; Yeh, Juddi; Rosen, Jeffrey M.

doi:10.1210/mend.13.2.0232

Cited by 124Cytokine Signaling Pathways and InteractionsEstrogen and related hormone effectsGrowth Hormone and Insulin-like Growth Factors

Glucocorticoid Receptor/Signal Transducer and Activator of Transcription 5 (STAT5) Interactions Enhance STAT5 Activation by Prolonging STAT5 DNA Binding and Tyrosine Phosphorylation

Wyszomierski, Shannon L., Yeh, Juddi, Rosen, Jeffrey M.·1999·Molecular Endocrinology

DOI 10.1210/mend.13.2.0232

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Abstract

The regulation of casein gene expression by both PRL and glucocorticoids has been a well studied paradigm for understanding how the signaling pathways regulated by these two hormones interact in the nucleus. Previous studies have demonstrated that the downstream effectors of these pathways, signal transducer and activator of transcription 5 (STAT5) and the glucocorticoid receptor (GR), are associated via protein-protein interactions and act synergistically to enhance beta-casein gene transcription. Indirect immunofluorescence microscopy was used to demonstrate that PRL-activated STAT5 can translocate GR into the nucleus, and that ligand-bound GR can translocate STAT5 into the nucleus. This provided further support of an interaction between the two proteins. To better understand the mechanism of transcriptional synergy between STAT5 and GR, experiments were performed in cells transiently transfected with STAT5 alone or with STAT5 and GR. GR cotransfection enhanced the DNA-binding activity of STAT5 without affecting STAT5 protein levels. The enhancement of STAT5 DNA binding by GR resulted in the formation of a complex that exhibited prolonged DNA binding after PRL treatment. This was correlated with increased STAT5 tyrosine phosphorylation, suggesting that GR enhances STAT5 DNA binding by modulating the rate of STAT5 dephosphorylation. In contrast, cotransfection of the estrogen receptor resulted in an overall decrease in STAT5 tyrosine phosphorylation, without changing the kin…

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A negative influence of DNA binding on Stat dephosphorylation was noted earlier also for Stat5.
“A negative influence of DNA binding on Stat dephosphorylation was noted earlier also for Stat5.”
From DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1 (2003) · cites this paper as Wyszomierski et al. 1999
Binding to the glucocorticoid receptor enhanced DNA binding of Stat5, which correlated with its prolonged tyrosine phosphorylation in vivo.
“Binding to the glucocorticoid receptor enhanced DNA binding of Stat5, which correlated with its prolonged tyrosine phosphorylation in vivo (Wyszomierski et al. 1999).”
From DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1 (2003) · cites this paper as Wyszomierski et al. 1999

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Authors: Wyszomierski, S. L., Yeh, J., & Rosen, J. M.
Affiliations: Baylor College of Medicine (US)
The University of Texas at San Antonio Health Science Center (US)
Corresponding author: Rosen, Jeffrey M.
ORCID: Rosen, Jeffrey M.
Venue: Molecular Endocrinology
Publisher: The Endocrine Society
Published: 1999-02
Volume: 13
Issue: 2
Pages: 330-343
ISSN: 0888-8809 (ISSN-L)
1944-9917
DOI: 10.1210/mend.13.2.0232
OpenAlex: W2091020488
Cited by: 124
References: 52
Citations by year: 2025: 1 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 1 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 4
FWCI: 3.72
Type: journal article
Language: en
Open access: closed
Locations: Molecular Endocrinology (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (CA-16303)
Topics: Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Growth Hormone and Insulin-like Growth Factors
Keywords: glucocorticoid receptor, STAT5, protein-protein interaction, transcriptional synergy, prolactin, nuclear translocation, estrogen receptor
MeSH terms: Animals, Caseins, Chlorocebus aethiops, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Cricetinae, Milk Proteins, Phosphorylation, Plasmids, Prolactin, Receptors, Estrogen, Receptors, Glucocorticoid, Transfection, Tyrosine, Blotting, Western, Trans-Activators, CHO Cells, Fluorescent Antibody Technique, Indirect, COS Cells, STAT5 Transcription Factor

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Glucocorticoid Receptor/Signal Transducer and Activator of Transcription 5 (STAT5) Interactions Enhance STAT5 Activation by Prolonging STAT5 DNA Binding and Tyrosine Phosphorylation

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Integrity signals

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