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Although signaling by the epidermal growth factor (EGF) receptor
is thought to be dependent on receptor tyrosine kinase activity, it is
clear that mitogen-activated protein (MAP) kinase can be activated by
receptors lacking kinase activity. Since analysis of the signaling
pathways used by kinase-defective receptors could reveal otherwise
masked capabilities, we examined in detail the tyrosine
phosphorylations and enzymes of the MAP kinase pathway induced by
kinase-defective EGF receptors. Following EGF stimulation of B82L cells
expressing a kinase-defective EGF receptor mutant (K721M), we found
that ERK2 and ERK1 MAP kinases, as well as MEK1 and MEK2 were all
activated, and SHC became prominently tyrosine-phosphorylated. By
contrast, kinase-defective receptors failed to induce detectable
phosphorylations of GAP (GTPase-activating protein), p62, JAK1, or
p91STAT1, all of which were robustly phosphorylated by wild-type
receptors. These data demonstrate that kinase-defective receptors
induce several protein tyrosine phosphorylations, but that these
represent only a subset of those seen with wild-type receptors. This
suggests that kinase-defective receptors activate a heterologous
tyrosine kinase with a specificity different from the EGF receptor. We
found that kinase-defective receptors induced ErbB2/c-Neu enzymatic
activation and ErbB2/c-Neu binding to SHC at a level even greater than
that induced by wild-type receptors. Thus, heterodimerization with and
activation of endogenous ErbB2/c-Neu is a possible mechanism by which
kinase-defective receptors stimulate the MAP kinase pathway.
Volume 270,
Number 20,
Issue of May 19, pp. 12085-12093, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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