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Vol. 273, Issue 2, 940-944, January 9, 1998
Protein Associates with Insulin Receptor Substrate 1 and Decreases Insulin-stimulated Phosphatidylinositol 3
-Kinase
Activity in 3T3L1 Adipocytes
From the Clinical Research Unit, Diabetes Center, Kyoto National
Hospital, Fushimi-ku, Kyoto 612, Japan, the § Department of
Medicine and Clinical Science, Kyoto University Graduate School of
Medicine, Sakyo-ku, Kyoto 606, Japan, and the ¶ Faculty of
Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606, Japan
The 14-3-3 protein family has been implicated in
growth factor signaling. We investigated whether 14-3-3 protein is
involved in insulin signaling in 3T3L1 adipocytes. A significant amount of insulin receptor substrate 1 (IRS-1) was immunodetected in the
immunoprecipitate with anti-14-3-3
antibody at the basal condition.
100 nM insulin increased the amount of IRS-1 in the immunoprecipitate 2.5-fold. The effect of insulin was abolished by 100 nM wortmannin. An in vitro binding study
revealed that glutathione S-transferase-14-3-3 fusion
protein directly associates with recombinant IRS-1. Pretreatment of
recombinant IRS-1 with alkaline phosphatase clearly decreased this
association. Because the recombinant IRS-1 was not phosphorylated on
its tyrosine residues, the results suggest that serine/threonine
phosphorylation of IRS-1 is responsible for the association. When the
cells are treated with insulin, phosphatidylinositol 3
-kinase (PI3K)
is supposed to complex either 14-3-3-IRS-1 or IRS-1. The
14-3-3-IRS-1-PI3K and IRS-1-PI3K complexes were separately prepared
by a sequential immunoprecipitation, first with anti-14-3-3 and then
with anti-IRS-1 antibodies. The specific activity of the PI3K in the
former was approximately half of that in the latter, suggesting that
14-3-3 protein bound to IRS-1 inhibits insulin-stimulated lipid
kinase activity of PI3K in 3T3L1 adipocytes.
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