Cited by 375Cytokine Signaling Pathways and InteractionsProtein Tyrosine PhosphatasesGenomics and Chromatin Dynamics

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STAT3β, a Splice Variant of Transcription Factor STAT3, Is a Dominant Negative Regulator of Transcription

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Caldenhoven, Eric, van Dijk, Thamar B., Solari, Roberto, Armstrong, John, Raaijmakers, Jan A.M., Lammers, Jan-Willem J., Koenderman, Leo, de Groot, Rolf P.·1996·Journal of Biological Chemistry

DOI 10.1074/jbc.271.22.13221

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Abstract

The 89-kDa STAT3 protein is a latent transcription factor which is activated in response to cytokines (interleukin (IL)-5 and -6) and growth factors (epidermal growth factor). Binding of IL-5 to its specific receptor activates JAK2 which leads to the tyrosine phosphorylation of STAT3 proteins. Here we report the cloning of a cDNA encoding a variant of the transcription factor STAT3 (named STAT3beta) which was isolated by screening an eosinophil cDNA library. Compared to wild-type STAT3, STAT3beta lacks an internal domain of 50 base pairs located near the C terminus. This splice product is a naturally occurring isoform of STAT3 and encodes a 80-kDa protein. We found by reconstitution of the human IL-5R in COS cells that like STAT3, STAT3beta is phosphorylated on tyrosine and binds to the pIRE from the ICAM-1 promoter after IL-5 stimulation. However, STAT3beta fails to activate a pIRE containing promoter in transient transfection assays. Instead, co-expression of STAT3beta inhibits the transactivation potential of STAT3. These results suggests that STAT3beta functions as a negative regulator of transcription.

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Self-citation
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Authors: Caldenhoven, E., van Dijk, T. B., Solari, R., Armstrong, J., Raaijmakers, J. A. M., Lammers, J.-W. J., Koenderman, L., & de Groot, R. P.
Affiliations: University Medical Center Utrecht (NL)
Corresponding author: de Groot, Rolf P.
ORCID: Solari, Roberto
Raaijmakers, Jan A.M.
Lammers, Jan-Willem J.
Koenderman, Leo
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1996-05
Volume: 271
Issue: 22
Pages: 13221-13227
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.271.22.13221
OpenAlex: W1495457417
Cited by: 373
References: 61
Citations by year: 2026: 4 · 2025: 3 · 2024: 8 · 2023: 6 · 2022: 6 · 2021: 10 · 2020: 7 · 2019: 9 · 2018: 10 · 2017: 7 · 2016: 8 · 2015: 6 · 2014: 14 · 2013: 10 · 2012: 8
FWCI: 11.54
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, 8934 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: STAT3β, transcription factors, dominant negative regulation, IL-5 receptor, eosinophils, transactivation inhibition, cytokine signaling, epidermal growth factor
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, DNA-Binding Proteins, Humans, Molecular Sequence Data, Phosphorylation, Repressor Proteins, RNA Splicing, Sequence Homology, Nucleic Acid, Transcription, Genetic, Tyrosine, Trans-Activators, DNA, Complementary, STAT3 Transcription Factor

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STAT3β, a Splice Variant of Transcription Factor STAT3, Is a Dominant Negative Regulator of Transcription

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