The Carboxyl-terminal Region of STAT3 Controls Gene Induction by the Mouse Haptoglobin Promoter
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Haptoglobin (HP) is one of the major acute phase plasma proteins in the mouse, and its synthesis is additively induced by interleukin (IL)-6 and glucocorticoids. STAT3 serves as the mediator of the IL-6 receptor signal and appears to contribute to the transcriptional induction of acute phase protein genes. The carboxyl-terminal region of STAT3, consisting of an acidic domain and containing a serine phosphorylation site, has been proposed to contribute to the induction process. To assess the role of STAT3 in the transcriptional control of the HP promoter, we applied two mutant forms of STAT3: one with a deletion of the carboxyl-terminal 55 amino acid residues, STAT3Delta55C, and the other with a substitution of serine 727 to alanine, STAT3SA. Like the wild-type STAT3, both mutant STAT3 forms are activated by the signal-transducing subunit of the IL-6 receptor, gp130, or by co-transfected IL-3 receptor. Ectopic expression and activation of wild-type STAT3 or STAT3SA in HepG2 hepatoma cells similarly enhance transcription through the IL-6-response element of the HP promoter. This enhancement is specific for STAT3 and cannot be reproduced by STAT1 or STAT5. In contrast, STAT3Delta55C inhibits IL-6-induced transcriptional activation. Interestingly, whereas receptor-activated STAT3 also enhances stimulation of the haptoglobin promoter by dexamethasone through the glucocorticoid receptor, activated STAT3Delta55C reduces the regulation below the level achieved by the glucocorticoid r…
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Mutation of STAT3 Ser727 to Ala modulates STAT3 transcriptional activity.
“Previous studies have reported that mutation of Ser727 in STAT3 to Ala modulates its transcriptional activity (Chung et al., 1997; Kim and Baumann, 1997; Lim and Cao, 1999; Wen et al., 1995; Yokogami et al., 2000).”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Kim and Baumann, 1997
STAT3 Ser phosphorylation plays a negative role in STAT3 nuclear dynamics and transcriptional activities.
“our study and others (Chung et al., 1997; Decker and Kovarik, 2000; Kim and Baumann, 1997) highlight a negative role of STAT3 Ser phosphorylation in STAT3 nuclear dynamics and transcriptional activities.”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Kim and Baumann, 1997
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Dispensable role for interferon‐γ in the burn‐induced acute phase response: A proteomic analysis
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Transmembrane Domain of gp130 Contributes to Intracellular Signal Transduction in Hepatic Cells
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STAT3 Regulation of Skeletal Muscle Wasting in Cancer Cachexia
Aydogdu, T. (2010)
Hatton, K. W. (2020) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2020.467
- Authors
- Kim, H., & Baumann, H.
- Affiliations
- Roswell Park Comprehensive Cancer Center (US)
- Corresponding author
- Baumann, Heinz
- ORCID
- Kim, Hongkyun
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-06
- Volume
- 272
- Issue
- 23
- Pages
- 14571-14579
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2036802237
- Cited by
- 68
- References
- 46
- Citations by year
- 2022: 1 · 2021: 1 · 2020: 4 · 2019: 2 · 2017: 2 · 2016: 1 · 2013: 4 · 2012: 1
- FWCI
- 2.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Roswell Park Cancer Institute
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK033886, DK 33886)
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- STAT3, C-terminal domain, acute phase proteins, IL-6 signaling, gp130, serine 727 phosphorylation, glucocorticoid receptor, dexamethasone, transcriptional activation, STAT1, STAT5
- MeSH terms
- Alanine, Animals, Base Sequence, Binding Sites, Dexamethasone, DNA-Binding Proteins, Haptoglobins, Humans, Kinetics, Phosphorylation, Promoter Regions, Genetic, Recombinant Fusion Proteins, Serine, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Signal Transduction, Trans-Activators, Antigens, CD, Interleukin-6, Receptors, Interleukin-3, Mutagenesis, Site-Directed, Point Mutation, Sequence Deletion, Receptors, Interleukin, COS Cells, Receptors, Interleukin-6, STAT3 Transcription Factor, Mice
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