Role of insulin receptor substrate-2 in interleukin-9-dependent proliferation

FEBS Lett. 2000 Oct 6;482(3):200-4. doi: 10.1016/s0014-5793(00)02059-7.


Interleukin-9 (IL-9) stimulation results in JAK, STAT and IRS1/2 phosphorylation. The role of IRS adaptor proteins in IL-9 signaling is not clear. We show that IL-9 induces IRS2 phosphorylation and association with phosphatidylinositol-3 kinase (PI 3-K) p85 subunit in TS1 cells and BaF/9R cells, which proliferate upon IL-9 stimulation. We observed a PI 3-K-dependent phosphorylation of protein kinase B (PKB) in TS1 cells, but not in BaF/9R, nor in other IL-9-dependent cell lines. Finally, 32D cells that were transfected with the IL-9 receptor but lack IRS expression survived in the presence of IL-9. Ectopic IRS1 expression allowed for IL-9-induced proliferation, in the absence of significant PKB phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Division / physiology*
  • Cells, Cultured
  • Extracellular Matrix Proteins / metabolism
  • Humans
  • Insulin Receptor Substrate Proteins
  • Interleukin-9 / physiology*
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphoproteins / biosynthesis
  • Phosphoproteins / physiology*
  • Phosphorylation
  • Protein-Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt


  • ECM1 protein, human
  • Ecm1 protein, mouse
  • Extracellular Matrix Proteins
  • IRS2 protein, human
  • Insulin Receptor Substrate Proteins
  • Interleukin-9
  • Intracellular Signaling Peptides and Proteins
  • Irs2 protein, mouse
  • Phosphoproteins
  • Proto-Oncogene Proteins
  • Phosphatidylinositol 3-Kinases
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt