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(Received for publication, March 19, 1996, and in revised form, August 16, 1996)
From the In this report, we demonstrate that insulin
receptor substrate-2 (IRS-2) is tyrosyl-phosphorylated following
stimulation of 3T3-F442A fibroblasts with growth hormone (GH), leukemia
inhibitory factor and interferon-
Volume 271, Number 46,
Issue of November 15, 1996
pp. 29415-29421
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
, and Leukemia Inhibitory Factor
Utilize Insulin Receptor Substrate-2 in Intracellular Signaling
,
,
Department of Physiology, The University of
Michigan Medical School, Ann Arbor, Michigan 48109-0622, the ** Joslin
Diabetes Center and Department of Medicine, Harvard Medical School,
Boston, Massachusetts 02215, the ¶ Center for BioTechnology,
Karolinska Institute, Novum, 141 57 Huddinge, Sweden, and the
Hagedorn Research Laboratory, Niels Steensensvej 6, DK-2820 Gentofte, Denmark
. In response to GH and leukemia
inhibitory factor, IRS-2 is immediately phosphorylated, with maximal
phosphorylation detected at 15 min; the signal is substantially
diminished by 60 min. In response to interferon-, tyrosine
phosphorylation of IRS-2 was prolonged, with substantial signal still
detected at 60 min. Characterization of the mechanism of signaling
utilized by GH indicated that tyrosine residues in GH receptor are not necessary for tyrosyl phosphorylation of IRS-2; however, the regions of
GH receptor necessary for IRS-2 tyrosyl phosphorylation are the same as
those required for JAK2 association and tyrosyl phosphorylation. The
role of IRS-2 as a signaling molecule for GH is further demonstrated by
the finding that GH stimulates association of IRS-2 with the 85-kDa
regulatory subunit of phosphatidylinositol 3
-kinase and with the
protein-tyrosine phosphatase SHP2. These results are consistent with
the possibility that IRS-2 is a downstream signaling partner of
multiple members of the cytokine family of receptors that activate JAK
kinases.
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