A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1
Open accessAbstract
The Stat1 activation-inactivation cycle involves phosphorylation of Stat1 in the cytoplasm, translocation to the nucleus, and then a return of the protein to the cytoplasm in a dephosphorylated state. However, the intracellular site of Stat1 dephosphorylation has not been determined. As receptor signaling declines, the flow of activated Stat1 molecules should be to the site of their dephosphorylation. We found that upon receptor-Janus kinase inactivation, either gradual or abruptly induced by staurosporine treatment, the flow of Stat1 was from cytoplasm to the nucleus and the nucleus was the final compartment in which phosphorylated Stat1 was detected. N-terminal mutants of Stat1, previously shown to remain phosphorylated for a longer time than wild-type Stat1, were able to enter the nucleus and were not inactivated in the presence of staurosporine, directly demonstrating that these mutations affect phosphatase access and/or activity during the normal dephosphorylation of Stat1. In the presence of sodium vanadate, a phosphatase inhibitor, phosphorylated Stat1 accumulated in the nucleus as the total amount of Stat1 in the cytoplasm declined to low levels. We conclude that the nucleus is the site of Stat1 inactivation and that dephosphorylation is required for the rapid nuclear export of Stat1.
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Possible tyrosine phosphatases include an unidentified nuclear tyrosine phosphatase activity that inactivates IFN-gamma-stimulated STAT-1 and the SH2-containing phosphatases SHP-1 and SHP-2, which regulate cytokine signals in other tissues.
“Possible tyrosine phosphatases include an unidentified nuclear tyrosine phosphatase activity that has been reported to inactivate IFN-γ-stimulated STAT-1 (37) and the SH2-containing phosphatases, SHP-1 and SHP-2, which regulate cytokine signals in other tissues (38).”
From Expression of suppressors of cytokine signaling during liver regeneration (2001) · cites this paper as [37]
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Cell Type-Specific and Tyrosine Phosphorylation-Independent Nuclear Presence of STAT1 and STAT3
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GATA-3 transcriptional imprinting in Th2 lymphocytes: A mathematical model
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P-STAT1 mediates higher-order chromatin remodelling of the human MHC in response to IFNγ
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STAT1 from the cell membrane to the DNA
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STAT signalling in cell proliferation and in development
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- Authors
- Haspel, R. L., & Darnell, J. E.
- Affiliations
- Rockefeller University (US)
- Laboratory of Molecular Cell Biology, The Rockefeller University, New York, NY 10021
- ORCID
- Haspel, Richard L.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-08-31
- Volume
- 96
- Issue
- 18
- Pages
- 10188-10193
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC17864
- OpenAlex
- W2120019133
- Cited by
- 203
- References
- 36
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 3 · 2017: 1 · 2015: 4 · 2014: 6 · 2013: 10 · 2012: 7
- FWCI
- 8.69
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA 09673, T32CA009673)
- National Institute of Allergy and Infectious Diseases (AI 32849, R37AI034420, AI 34420, R01AI032489)
- Topics
- Health Sciences › Medicine › Oncology › 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 › Protein Kinase Regulation and GTPase Signaling
- Keywords
- STAT1, protein tyrosine phosphatase, nuclear export, Janus kinase, staurosporine, nuclear translocation, sodium vanadate, transcription factor regulation
- MeSH terms
- Animals, Cell Line, Cell Nucleus, DNA-Binding Proteins, Humans, Kinetics, Phosphorylation, Protein-Tyrosine Kinases, Recombinant Proteins, Transfection, Vanadates, Signal Transduction, Trans-Activators, Mutagenesis, Site-Directed, Protein Tyrosine Phosphatases, Staurosporine, STAT1 Transcription Factor, Mice
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