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J. Biol. Chem., Vol. 269, Issue 44, 27315-27321, Nov, 1994
JE Peterson, T Jelinek, M Kaleko, K Siddle and MJ Weber
Using a panel of src mutants partially defective for malignant
transformation, our laboratory has previously identified the insulin- like
growth factor (IGF-I) receptor as a protein whose tyrosine phosphorylation
correlates with transformation by src in embryonic chick cells (Kozma et
al., 1990; Kozma and Weber, 1990). It has not been clear, however, whether
src-induced phosphorylation altered the enzymatic or signaling properties
of the IGF-I receptor and thus whether the IGF-I receptor could be a
functionally significant target for pp60v-src. To examine the effect of src
expression on the activity of the IGF-I receptor, the human IGF-I receptor
was expressed in Rat-1 fibroblasts co-expressing the temperature-sensitive
v-src mutant, tsLA29. The IGF-I receptor exhibited an elevated level of
tyrosine phosphorylation in src transformed cells even in the absence of
IGF-I treatment. Increased receptor phosphorylation occurred rapidly when
cells expressing a temperature-conditional src mutant were shifted from the
restrictive to the permissive temperature. Src-induced phosphorylation of
the receptor was correlated with an increase in the in vitro tyrosine
kinase activity of the receptor, both toward itself and exogenous
substrates. The src-induced increase in receptor activity was shown to be
dependent on tyrosine phosphorylation, as treatment with a
tyrosine-specific phosphatase lowered receptor activity. A kinase-defective
mutant of the IGF-I receptor also became constitutively phosphorylated in
src-transformed cells, ruling out a possible autocrine mechanism for this
phosphorylation. Collectively these data indicate that pp60v-src induces
ligand-independent phosphorylation and activation of the IGF-I receptor by
an intracellular mechanism, consistent with the possibility that receptor
phosphorylation could contribute to the genesis of the transformed
phenotype.
c phosphorylation and activation of the IGF-I receptor in src- transformed cells
Department of Microbiology, University of Virginia, Charlottesville 22908.
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