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J. Biol. Chem., Vol. 275, Issue 29, 22583-22589, July 21, 2000
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From the Department of Medicine, Duke University Medical Center,
Durham, North Carolina 27710
The receptor for insulin-like growth factor
1 (IGF-1) mediates multiple cellular responses, including stimulation
of both proliferative and anti-apoptotic pathways. We have examined the role of cross talk between the IGF-1 receptor (IGF-1R) and the epidermal growth factor receptor (EGFR) in mediating responses to
IGF-1. In COS-7 cells, IGF-1 stimulation causes tyrosine
phosphorylation of the IGF-1R
Transactivation of the EGF Receptor Mediates IGF-1-stimulated Shc
Phosphorylation and ERK1/2 Activation in COS-7 Cells*
subunit, the EGFR, insulin receptor
substrate-1 (IRS-1), and the Shc adapter protein. Shc
immunoprecipitates performed after IGF-1 stimulation contain
coprecipitated EGFR, suggesting that IGF-1R activation induces the
assembly of EGFR·Shc complexes. Tyrphostin AG1478, an inhibitor of
the EGFR kinase, markedly attenuates IGF-1-stimulated phosphorylation
of EGFR, Shc, and ERK1/2 but has no effect on phosphorylation of
IGF-1R, IRS-1, and protein kinase B (Akt). Cross talk between IGF-1 and
EGF receptors is mediated through an autocrine mechanism involving
matrix metalloprotease-dependent release of heparin-binding
EGF (HB-EGF), because IGF-1-mediated ERK activation is inhibited both
by [Glu52]Diphtheria toxin, a specific
inhibitor of HB-EGF, and the metalloprotease inhibitor
1,10-phenanthroline. These data demonstrate that IGF-1 stimulation of
the IRS-1/PI3K/Akt pathway and the EGFR/Shc/ERK1/2 pathway occurs by
distinct mechanisms and suggest that IGF-1-mediated "transactivation" of EGFR accounts for the majority of
IGF-1-stimulated Shc phosphorylation and subsequent activation of the
ERK cascade.
*
This work was supported by National Institutes of Health
Grants DK02352 and DK55524 (to L. M. L.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Medicine, Box
3821, Duke University Medical Center, Durham, NC 27710. Tel.:
919-684-2974; Fax: 919-684-8875; E-mail:
Luttrell@receptor-biol.duke.edu.
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