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Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases.

The signaling molecules insulin receptor substrate (IRS)-1 and the newly described IRS-2 (4PS) molecule are major insulin and interleukin 4 (IL-4)-dependent phosphoproteins. We report here that IL-2, IL-7, and IL-15, as well as IL-4, rapidly stimulate the tyrosine phosphorylation of IRS-1 and IRS-2 in human peripheral blood T cells, NK cells, and in lymphoid cell lines. In addition, we show that the Janus kinases, JAK1 and JAK3, associate with IRS-1 and IRS-2 in T cells. Coexpression studies demonstrate that these kinases can tyrosine-phosphorylate IRS-2, suggesting a possible mechanism by which cytokine receptors may induce the tyrosine phosphorylation of IRS-1 and IRS-2. We further demonstrate that the p85 subunit of phosphoinositol 3-kinase associates with IRS-1 in response to IL-2 and IL-4 in T cells. Therefore, these data indicate that IRS-1 and IRS-2 may have important roles in T lymphocyte activation not only in response to IL-4, but also in response to IL-2, IL-7, and IL-15.

Pubmed ID: 7499365

Authors

  • Johnston JA
  • Wang LM
  • Hanson EP
  • Sun XJ
  • White MF
  • Oakes SA
  • Pierce JH
  • O'Shea JJ

Journal

The Journal of biological chemistry

Publication Data

December 1, 1995

Associated Grants

None

Mesh Terms

  • Humans
  • Insulin Receptor Substrate Proteins
  • Interleukins
  • Intracellular Signaling Peptides and Proteins
  • Janus Kinase 1
  • Janus Kinase 3
  • Phosphoproteins
  • Phosphorylation
  • Protein-Tyrosine Kinases
  • T-Lymphocytes
  • Tyrosine