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Volume 272, Number 2, Issue of January 10, 1997 pp. 1377-1381
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Insulin Receptor Substrate-2 Is the Major 170-kDa Protein Phosphorylated on Tyrosine in Response to Cytokines in Murine Lymphohemopoietic Cells

(Received for publication, June 5, 1996, and in revised form, November 1, 1996)

Melanie J. Welham Dagger § , Heather Bone Dagger § , Megan Levings Dagger , Leslie Learmonth Dagger , Ling-Mei Wang par , Kevin B. Leslie Dagger , Jacalyn H. Pierce par and John W. Schrader Dagger

From the Dagger  The Biomedical Research Centre, 2222 Health Sciences Mall, University of British Columbia, Vancouver, British Columbia, V6T 1Z3 Canada, § The Pharmacology Group, School of Pharmacy and Pharmacology, University of Bath, Bath, BA2 7AY United Kingdom, and the par  Laboratory of Cell and Molecular Biology, National Institutes of Health, Bethesda, Maryland 20892

Insulin receptor substrate 1 (IRS-1), and its structural relative IRS-2, are both phosphorylated on tyrosine following treatment of cells with interleukin-4 (IL-4) and insulin. We have investigated whether both IRS-1 and IRS-2 are expressed in murine lymphohemopoietic cells. T and B lymphocytes and macrophages from primary cultures expressed only IRS-2, which became phosphorylated on tyrosine following stimulation with both IL-4 and insulin. Likewise, the murine myeloid cell line FD-5 expressed only IRS-2, which was tyrosine phosphorylated in response to IL-4 and insulin, as well as interleukin-3 and granulocyte-macrophage colony stimulating factor. Neither IRS-1 nor IRS-2 were expressed at detectable levels in primary bone marrow mast cells although these cells do respond to IL-4. Moreover, a factor-dependent lymphocyte cell line, CT.4S, which grows continuously in IL-4, did not express detectable levels of IRS-1 or IRS-2. IRS-2 from FD-5 cells stimulated with either IL-4 or insulin bound to glutathione S-transferase fusion proteins of the p85 subunit of phosphoinositol 3'-kinase, Grb2, and Syp, paralleling reported associations of IRS-1 with these molecules and indicating phosphorylation of the corresponding residues on IRS-2.


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