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J. Biol. Chem., Vol. 268, Issue 21, 15536-15543, Jul, 1993
P Morrison, K Takishima and MR Rosner
Epidermal growth factor (EGF) receptor tyrosine kinase activity is down-
regulated by a number of growth-modulating agents that activate protein
kinase C and/or mitogen-activated protein (MAP) kinases. Although the
mechanism is unclear, it has been hypothesized that phosphorylation of
specific threonine residues leads to inhibition of the EGF receptor
tyrosine kinase. Two sites phosphorylated on the EGF receptor in response
to phorbol esters are possible mediators of this effect: threonine 654, the
target of protein kinase C, and threonine 669, the target of MAP kinase and
the major site of phosphorylation on the EGF receptor. In order to
investigate the role of these residues in receptor regulation, we
substituted glutamic acid to mimic the negative charge introduced by
phosphorylation at these sites. The wild-type and mutant receptor cDNAs
were then transfected into CHO cells that lack endogenous EGF receptor. The
EGF binding properties of the mutant receptors were similar to those of the
wild-type EGF receptors. EGF stimulated tyrosine kinase activity and DNA
synthesis in cells expressing both mutant receptors, indicating that the
mutant EGF receptors are biologically active. Treatment of cells with
phorbol esters inhibited the high affinity EGF binding and tyrosine kinase
activities of both mutant and wild-type EGF receptors. These results
indicate that acidic residues at either the Thr-654 or Thr-669 site
modulate but do not block EGF receptor signalling. Furthermore, this data
demonstrates that the mutant EGF receptors are still a target for
inhibition by phorbol esters. Thus, events other than phosphorylation of
Thr-654 or Thr-669 appear to be required for receptor down- regulation by
protein kinase C or MAP kinase.
Role of threonine residues in regulation of the epidermal growth factor receptor by protein kinase C and mitogen-activated protein kinase
Ben May Institute, University of Chicago, Illinois.
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