Tyrosine phosphorylation of DNA binding proteins by multiple cytokines.

@article{Larner1993TyrosinePO,
  title={Tyrosine phosphorylation of DNA binding proteins by multiple cytokines.},
  author={Andrew C. Larner and Muriel D David and Gerald M. Feldman and Ken-ichi Igarashi and Rebeccahawes Hackett and Deborah S.A. Webb and Sharon M. Sweitzer and Emanuel F. Petricoin and David S. Finbloom},
  journal={Science},
  year={1993},
  volume={261 5129},
  pages={
          1730-3
        }
}
Interferon-alpha (IFN-alpha) and IFN-gamma regulate gene expression by tyrosine phosphorylation of several transcription factors that have the 91-kilodalton (p91) protein of interferon-stimulated gene factor-3 (ISGF-3) as a common component. Interferon-activated protein complexes bind enhancers present in the promoters of early response genes such as the high-affinity Fc gamma receptor gene (Fc gamma RI). Treatment of human peripheral blood monocytes or basophils with interleukin-3 (IL-3), IL-5… 
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Rapid activation of proteins that interact with the interferon gamma activation site in response to multiple cytokines
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Data suggest a pathway by which cytokines induce rapid changes in gene expression, and transcriptional activation of a reporter gene linked to a synthetic IFN gamma-responsive promoter is observed in response toIFN gamma, IL-6, and LIF.
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Protein kinases of the Jak family were rapidly tyrosine phosphorylated, and both APRF and Jak1 associated with gp130, indicating that Jak family protein kinases may participate in IL-6 signaling and that APRF may be activated in a complex withgp130.
Rapid activation of the interferon-gamma signal transduction pathway by inhibitors of tyrosine phosphatases.
TLDR
It is found that in the absence of interferon-gamma, treatment of cells with an inhibitor of tyrosine phosphatases causes a rapid and potent activation of the components of the interfer on-board signal transduction pathway and induces an interferonsgamma-responsive gene.
Cytokines and growth factors signal through tyrosine phosphorylation of a family of related transcription factors.
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TLDR
Sequence analysis of a cDNA encoding a polypeptide recognizing specifically the MATE motif led to the identification of this product as the proto-oncogene PU.1/Spi-1, a transcriptional activator expressed in myeloid and B cells.
Interleukin-5 signaling in human eosinophils involves JAK2 tyrosine kinase and Stat1 alpha.
TLDR
IL-5 induced rapid and transient tyrosine phosphorylation of JAK2 and two DNA-binding complexes in human eosinophils, including Stat1 alpha, showing for the first time that molecular mechanisms of IL-5 signaling inhuman eosInophils involve members of the JAK kinase family as well as members ofThe Stat family.
Characterization of the Interleukin-4 Nuclear Activated Factor/STAT and Its Activation Independent of the Insulin Receptor Substrate Proteins (*)
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Delayed tyrosine phosphorylation and nuclear expression of STAT1 following antigen receptor stimulation of B lymphocytes.
TLDR
STAT1 alpha plays a dynamic role in the composition of IRF-1 promoter-specific DNA binding complexes stimulated by B cell Ag receptor ligation, and nuclear expression of phosphorylated STAT1 alpha is regulated in a unique fashion by Ag receptor engagement.
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References

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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
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TLDR
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