Maximal activation of transcription by statl and stat3 requires both tyrosine and serine phosphorylation

@article{Wen1995MaximalAO,
  title={Maximal activation of transcription by statl and stat3 requires both tyrosine and serine phosphorylation},
  author={Zilong Wen and Zhong Zhong and James E. Darnell},
  journal={Cell},
  year={1995},
  volume={82},
  pages={241-250}
}

Figures from this paper

STATs in Cytokine-mediated Transcriptional Regulation
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The current understanding of the functional domains, the regulation, and the physiological roles of STATs in cytokine signaling are reviewed.
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This review addresses recent advances in understanding the regulation of STAT serine phosphorylation, as well as the kinases and other signal transducers implied in this process.
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The authors state that the CDK8 module of the Mediator complex is a key component in the STAT1 signal pathway, linking serine phosphorylation to gene-specific transcriptional events.
Stat1 serine phosphorylation occurs independently of tyrosine phosphorylation and requires an activated Jak2 kinase
TLDR
Evidence is presented that Stat1 tyrosineosphorylation is not a prerequisite for Stat1 serine phosphorylation, although an active Jak2 kinase is required for both phosphorylated events.
STAT3 Is a Serine Kinase Target in T Lymphocytes
TLDR
The results show that STAT3 proteins are targets for multiple kinase pathways in T cells and can integrate signals from both cytokine receptors and antigen receptors, and it is shown that H-7-sensitive kinases do not regulate STAT3 tyrosine phosphorylation or phosphorylated of serine 727.
Regulation of Stat3 Activation by MEK Kinase 1*
TLDR
A novel role of MEKK1 to modulate tyrosine kinases that results in the activation of specific members of STAT family is demonstrated for the first time.
Simultaneous tyrosine and serine phosphorylation of STAT3 transcription factor is involved in Rho A GTPase oncogenic transformation.
TLDR
Results indicate that Stat3 is an important player in RhoA-mediated oncogenic transformation, which requires simultaneous phosphorylation at both tyrosine and serine residues by specific signaling events triggered by Rho a effectors.
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References

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Serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3, a member of the interleukin-6 family of cytokines, which binds to and activate receptors that contain a common subunit, gp130.
A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma.
Interferon-gamma (IFN-gamma) stimulates transcription of specific genes by inducing tyrosine phosphorylation of a 91-kilodalton cytoplasmic protein (termed STAT for signal transducer and activator of
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TLDR
A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor and interleukin-6 but not interferon gamma (IFN-gamma).
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TLDR
Evidence is presented that a heterodimer of Stat1 and Stat2 is present in ISGF3 and that Stat 1 and the 48-kDa protein make precise contact, while Stat2 makes general contact, with the interferon-stimulated response element, the binding site of the IsGF3.
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TLDR
Using cell lines lacking the Stat91 or Stat84 proteins, it is shown that mutations in several different sites in the 91-kDa protein block the interferon alpha-induced phosphorylation of the 91/84 protein and subsequent ISGF-3 formation.
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TLDR
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TLDR
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TLDR
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TLDR
Comparison with the deduced protein sequence of the two previously described genes (Stat91 and Stat113), discovered because of their activation as transcription factors after interferon-induced tyrosine phosphorylation, shows several highly conserved regions, including the putative SH3 and SH2 domains.
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