Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3.

@article{Woetmann1999InhibitionOP,
  title={Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3.},
  author={Anders Woetmann and Mette Weidinger Nielsen and S\oren Tvorup Christensen and Johannes Brockdorff and Keld Kaltoft and April Engel and S\oren Skov and Christine Brender and Carsten Geisler and Arne Svejgaard and J\orgen Rygaard and Vagn Leick and N Joey Odum},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 19},
  pages={10620-5}
}
Signal transducers and activators of transcription (STATs) are rapidly phosphorylated on tyrosine residues in response to cytokine and growth factor stimulation of cell surface receptors. STATs hereafter are translocated to the nucleus where they act as transcription factors. Recent reports suggest that serine phosphorylation of STATs also is involved in the regulation of STAT-mediated gene transcription. Here, we studied the role of serine/threonine phosphatases in STAT3 signaling in human… CONTINUE READING
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