Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR

@article{Yokogami2000SerinePA,
  title={Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR},
  author={K. Yokogami and S. Wakisaka and J. Avruch and S. Reeves},
  journal={Current Biology},
  year={2000},
  volume={10},
  pages={47-50}
}
Neuropoletic cytokines such as ciliary neurotrophic factor (CNTF) can activate multiple signaling pathways in parallel, including those involving Janus kinase (JAK)-signal transducers and activators of transcription (STATs), mitogen-activated protein kinase (MAPK), phosphatidylinositol 3-kinase (PI 3-kinase) and mammalian target of rapamydn (mTOR)-p70 S6 kinase . Crosstalk occurs between these pathways, because studies have shown that STAT3 requires phosphorylation on tyrosine and serine… Expand
MSK1 and JNKs Mediate Phosphorylation of STAT3 in UVA-irradiated Mouse Epidermal JB6 Cells*
Mitochondrial Localized STAT3 Is Involved in NGF Induced Neurite Outgrowth
The role of phosphorylation in the regulation of the mammalian target of rapamycin.
The YXXQ motif in gp 130 is crucial for STAT3 phosphorylation at Ser727 through an H7-sensitive kinase pathway
Kinase activities associated with mTOR.
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