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J Biol Chem, Vol. 273, Issue 8, 4672-4680, February 20, 1998
From the Joslin Diabetes Center, Harvard Medical School,
Boston, Massachusetts 02215
Insulin-like growth factor-I (IGF-I) receptors
activate divergent signaling pathways by phosphorylating multiple
cellular proteins, including insulin receptor substrate-1 (IRS-1) and
the Shc proteins. Following hormone binding, IGF-I receptors cluster into clathrin-coated pits and are internalized via an endocytotic mechanism. This study investigates the relationship between IGF-I receptor internalization and signaling via IRS-1 and Shc. A mutation in
the C terminus of the IGF-I receptor decreased both the rate of
receptor internalization and IGF-I-stimulated Shc phosphorylation by
more than 50%, but did not affect IRS-1 phosphorylation. Low temperature (15 °C) decreased IGF-I receptor internalization and completely inhibited Shc phosphorylation. Although receptor and IRS-1
phosphorylation were decreased in accordance with delayed binding
kinetics at 15 °C, the ratio of IRS-1 to receptor phosphorylation was increased more than 2-fold. Dansylcadaverine decreased receptor internalization and Shc phosphorylation, but did not change receptor or
IRS-1 phosphorylation. Consistent with these findings, dansylcadaverine inhibited IGF-I-stimulated Shc-Grb2 association, mitogen-activated protein kinase phosphorylation, and p90 ribosomal S6 kinase activation, but did not affect the association of phosphatidylinositide 3-kinase with IRS-1 or activation of p70 S6 kinase. These data support the
concept that Shc/mitogen-activated protein kinase pathway activation
requires IGF-I receptor internalization, whereas the IRS-1 pathway is
activated by both cell surface and endosomal receptors.
Insulin-like Growth Factor-I Receptor Internalization Regulates
Signaling via the Shc/Mitogen-activated Protein Kinase Pathway, but Not
the Insulin Receptor Substrate-1 Pathway
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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