Cited by 312Cytokine Signaling Pathways and InteractionsProtein Tyrosine Phosphatasesinterferon and immune responses

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The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.

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Haspel, R. L., Salditt‐Georgieff, M., Darnell, J. E.·1996·The EMBO Journal

DOI 10.1002/j.1460-2075.1996.tb01016.xPMC PMC452449

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Abstract

After interferon-gamma (IFN-gamma) treatment of cells the appearance of tyrosine phosphorylated Stat1 in the nucleus was maximal within 20-30 min, remained for 2-2.5 h and activated molecules disappeared by 4 h. In the absence of continued signaling from the receptor (imposed by staurosporine treatment) previously activated Stat1 disappeared completely within 60 min, implying continuous generation and removal of active molecules during extended IFN-gamma treatment. Proteasome inhibitors prolonged the time of activation of Stat1 by prolonging signaling from the receptor but not by blocking removal of already activated Stat1 molecules. By analyzing with 35S labeling the distribution of total Stat1 and activated Stat1, we concluded that the Stat1 molecules promptly cycle into the nucleus as tyrosine phosphorylated molecules and later return quantitatively to the cytoplasm as non-phosphorylated molecules. Therefore, the removal of the activated Stat1 molecules from the nucleus appears not to be proteolytic but must depend on a protein tyrosine phosphatase(s).

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Authors: Haspel, R. L., Salditt‐Georgieff, M., & Darnell, J. E.
Affiliations: Rockefeller University (US)
ORCID: Haspel, R. L.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1996-11-01
Volume: 15
Issue: 22
Pages: 6262-6268
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1996.tb01016.x
PMC: PMC452449
OpenAlex: W1702674772
Cited by: 312
References: 41
Citations by year: 2026: 2 · 2025: 1 · 2023: 1 · 2022: 1 · 2021: 5 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 1 · 2016: 3 · 2015: 4 · 2014: 12 · 2013: 9 · 2012: 6
FWCI: 12.59
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (GM07739)
National Institute of Allergy and Infectious Diseases (R01AI032489, AI32489, AI324420)
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 › Immunology and Microbiology › Immunology › interferon and immune responses
Keywords: STAT1, tyrosine phosphorylation, protein tyrosine phosphatase, interferon-gamma signaling, nuclear translocation, proteasome inhibitors, staurosporine, receptor signaling, transcription factor regulation
MeSH terms: Acetylcysteine, Cell Nucleus, Cysteine Endopeptidases, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Enzyme Inhibitors, Fibroblasts, Humans, Interferon-gamma, Leupeptins, Multienzyme Complexes, Nuclear Proteins, Phosphorylation, Vanadates, Blotting, Western, Signal Transduction, Trans-Activators, Protein Tyrosine Phosphatases, Receptors, Interferon, Phosphotyrosine, Staurosporine, Proteasome Endopeptidase Complex, STAT1 Transcription Factor

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The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.

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