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

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  • A. WoetmannM. Nielsen N. Odum
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
TLDR
Evidence is provided that PP2A plays a crucial role in the regulation of STAT3 phosphorylation and subcellular distribution in T cells and suggests that the level of STAT2A phosphorylated is balanced between a staurosporine-sensitive kinase(s) and PP1/PP2A.
Stat5a Serine Phosphorylation
TLDR
It is shown that mutagenesis of Ser725, Ser779, or a combination ofSer725/779 to an Ala had no effect on prolactin-induced transcriptional activation of a β-casein reporter construct, and the results suggest that Ser725 phosphorylation has an impact on signal duration.
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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.
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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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