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(Received for publication, August 7, 1996, and in revised form, September 24, 1996)
From the Department of Microbiology, University of Virginia Health
Sciences Center, Charlottesville, Virginia 22908
The insulin-like growth factor type I (IGF-I)
receptor can become tyrosine phosphorylated and enzymatically activated
either in response to ligand or because of the activity of the Src
tyrosine kinase (Peterson, J. E., Jelinek, T., Kaleko, M., Siddle, K., and Weber, M. J. (1994) J. Biol. Chem. 269, 27315-27321). The goal of the present study was to analyze the
mechanistic basis and functional significance of the Src-induced
phosphorylation and activation of the IGF-I receptor. 1) We mapped the
sites of IGF-I receptor autophosphorylation to peptides representing
three different receptor domains: tyrosines 943 and 950 in the
juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase
domain; and tyrosine 1316 in the carboxyl-terminal domain. The
juxtamembrane and kinase-domain peptides were phosphorylated both
in vivo and in vitro. The carboxyl-terminal
site, although phosphorylated in vitro and in
src-transformed cells, was not a major site of ligand-induced phosphorylation in vivo. 2) We determined
that the sites of Src-induced phosphorylation of the IGF-I receptor are
the same as the ligand-induced autophosphorylation sites and that the
Src kinase can catalyze these phosphorylations directly. 3) We showed
that cells cultured from mice in which the IGF-I receptor has been
knocked out by homologous recombination are defective for morphological
transformation by src. Thus, the Src kinase can substitute
for the receptor kinase in phosphorylating and activating the IGF-I
receptor, and this receptor phosphorylation and activation are
essential for transformation by src.
Volume 271, Number 49,
Issue of December 6, 1996
pp. 31562-31571
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
REQUIREMENT FOR TRANSFORMATION BY src
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