Insulin-induced serine phosphorylation of IRS-2 via ERK1/2 and mTOR: studies on the function of Ser675 and Ser907.

@article{Fritsche2011InsulininducedSP,
  title={Insulin-induced serine phosphorylation of IRS-2 via ERK1/2 and mTOR: studies on the function of Ser675 and Ser907.},
  author={Louise Fritsche and Sabine S. Neukamm and Rainer Lehmann and Elisabeth Kremmer and Anita M. Hennige and Andrea Hunder-Gugel and Martin Schenk and Hans-Ulrich H{\"a}ring and Erwin D. Schleicher and Cora Weigert},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2011},
  volume={300 5},
  pages={E824-36}
}
The identity of specific serine phosphorylation residues of insulin receptor substrate (IRS)-2 and their impact on insulin signal transduction are largely unknown. Ser(675) and Ser(907) of mouse IRS-2 are adjacent to PI 3-kinase or Grb2 binding domains, respectively. Using monoclonal phosphosite-specific antibodies, we demonstrated the phosphorylation of both serines after stimulation of Fao hepatoma cells with insulin, anisomycin, or phorbol esters. Phosphorylation of both sites was a late and… CONTINUE READING
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Interplay and effects of temporal changes in E835 PHOSPHORYLATION OF Ser675 AND Ser907 OF IRS-2 AJP-Endocrinol Metab

  • C Weigert, M Kron, +5 authors R. Lehmann
  • MAY
  • 2011
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