Cited by 268Cytokine Signaling Pathways and Interactionsinterferon and immune responsesGenomics and Chromatin Dynamics

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Stat1 Depends on Transcriptional Synergy with Sp1

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Look, Dwight C., Pelletier, Mark R., Tidwell, Rose M., Roswit, William T., Holtzman, Michael J.·1995·Journal of Biological Chemistry

DOI 10.1074/jbc.270.51.30264

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Abstract

STAT (signal transducer and activator of transcription) proteins combine with cytokine receptors and receptor-associated kinases in distinct protein/protein interactions that are critical for STAT-dependent signal transduction events, but the nature of any subsequent STAT interactions with DNA-binding proteins in the nucleus is less certain. Based on assays of DNA/protein binding and activity of transfected reporter plasmids, we determined that occupation of contiguous DNA-binding sites for Stat1 (the first member of the STAT family) and the transcriptional activator Sp1 are both required for full activation of the intercellular adhesion molecule-1 gene by interferon-gamma. Thus, Stat1 binding to DNA cannot by itself be equated with biologic actions of Stat1. In co-immunoprecipitation experiments, we also obtained evidence of direct and selective Stat1/Sp1 interaction (in primary culture cells without overexpression), further indicating that Stat1/Sp1 synergy confers an element of specificity in the pathway leading to cytokine-activated transcription and cytokine-dependent immunity and inflammation.

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Authors: Look, D. C., Pelletier, M. R., Tidwell, R. M., Roswit, W. T., & Holtzman, M. J.
Affiliations: Washington University in St. Louis (US)
Corresponding author: Holtzman, Michael J.
ORCID: Holtzman, Michael J.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1995-12
Volume: 270
Issue: 51
Pages: 30264-30267
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.270.51.30264
OpenAlex: W2129362876
Cited by: 268
References: 36
Citations by year: 2026: 1 · 2025: 1 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 3 · 2014: 1 · 2013: 2 · 2012: 5
FWCI: 8.74
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, 9117 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hl040078-10)
National Heart, Lung, and Blood Institute (HL-40078, HL 07317, HL/AI-51071, T32HL007317)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: STAT1, Sp1, transcriptional synergy, interferon-gamma, DNA binding sites, transcriptional activation, cytokine signaling
MeSH terms: Animals, Base Sequence, Binding Sites, Cell Line, DNA-Binding Proteins, Humans, Interferon-gamma, Luciferases, Molecular Sequence Data, Oligodeoxyribonucleotides, Recombinant Fusion Proteins, Recombinant Proteins, Repetitive Sequences, Nucleic Acid, Transcription, Genetic, Transfection, Signal Transduction, Chloramphenicol O-Acetyltransferase, Trans-Activators, Gene Expression, Polymerase Chain Reaction, Intercellular Adhesion Molecule-1, STAT1 Transcription Factor

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Stat1 Depends on Transcriptional Synergy with Sp1

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