Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor
Abstract
The interferon-alpha (IFN-alpha)-stimulated gene factor 3 (ISGF3), a transcriptional activator, contains three proteins, termed ISGF3 alpha proteins, that reside in the cell cytoplasm until they are activated in response to IFN-alpha. Treatment of cells with IFN-alpha caused these three proteins to be phosphorylated on tyrosine and to translocate to the cell nucleus where they stimulate transcription through binding to IFN-alpha-stimulated response elements in DNA. IFN-gamma, which activates transcription through a different receptor and different DNA binding sites, also caused tyrosine phosphorylation of one of these proteins. The ISGF3 alpha proteins may be substrates for one or more kinases activated by ligand binding to the cell surface and may link occupation of a specific polypeptide receptor with activation of transcription of a set of specific genes.
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T lymphocyte lineage-specific STAT3-KO mice studies revealed a crucial role of IL-6/STAT3-mediated T cell survival independent of Bcl-2.
“T lymphocyte lineage-specific STAT3-KO mice studies revealed the crucial role of IL-6/STAT3-mediated T cell survival, independent of Bcl-2”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as Schindler et al., 1992
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- Authors
- Schindler, C., Shuai, K., Prezioso, V. R., & Darnell, J. E.
- Affiliations
- Rockefeller University (US)
- Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.
- ORCID
- Shuai, Ke
- Venue
- Science
- Published
- 1992-08-07
- Volume
- 257
- Issue
- 5071
- Pages
- 809-813
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1965398762
- Cited by
- 899
- References
- 1
- Citations by year
- 2026: 9 · 2025: 7 · 2024: 16 · 2023: 15 · 2022: 12 · 2021: 9 · 2020: 21 · 2019: 14 · 2018: 10 · 2017: 14 · 2016: 18 · 2015: 16 · 2014: 20 · 2013: 25 · 2012: 25
- FWCI
- 39.16
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM007982, GM07982-10)
- National Institute of Allergy and Infectious Diseases (R01AI032489, AI32489)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- interferon-alpha, ISGF3, tyrosine phosphorylation, transcription factor activation, nuclear translocation, interferon-stimulated response element, interferon-gamma, transcriptional activation, receptor kinase signaling
- MeSH terms
- Cell Membrane, Cell Nucleus, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Fluorescent Antibody Technique, HeLa Cells, Humans, Interferon-gamma, Methionine, Models, Biological, Molecular Weight, Phosphopeptides, Phosphorylation, Protease Inhibitors, Protein-Tyrosine Kinases, Transcription Factors, Transcription, Genetic, Tyrosine, Interferon-alpha, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, alpha Subunit, Interferon-Stimulated Gene Factor 3, gamma Subunit
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