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Epidermal growth factor and its receptor.

G N Gill, P J Bertics, J B Santon

Molecular and Cellular Endocrinology

|June 1, 1987

Summary

Epidermal growth factor (EGF) receptor regulation is crucial for normal cell growth. Aberrant regulation, like gene amplification, contributes to human tumors and uncontrolled cell proliferation.

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Area of Science:

Molecular Biology
Cell Signaling
Oncology

Background:

Epidermal growth factor (EGF) binds its receptor, activating tyrosine protein kinase activity.
EGF receptor gene amplification and overexpression are observed in human tumors, suggesting oncogenic potential.
EGF receptor activity is tightly regulated by synthesis, degradation, and phosphorylation.

Purpose of the Study:

To elucidate the regulatory mechanisms of the EGF receptor.
To understand how dysregulation of EGF receptor contributes to human cancers.

Main Methods:

Analysis of EGF receptor gene expression in human tumors.
Investigating the role of phosphorylation in EGF receptor activity.
Studying the effects of protein kinase C on EGF receptor function.

Main Results:

Intramolecular self-phosphorylation at Tyr1173 enhances substrate phosphorylation.
Phosphorylation at Thr654 by protein kinase C reduces EGF binding and kinase activity.
Dysregulation of these controls leads to uncontrolled cell growth, similar to erb B transformation.

Conclusions:

The EGF receptor is extensively regulated at multiple levels.
Abrogation of these regulatory controls is implicated in human tumor development.
Understanding EGF receptor regulation offers insights into cancer pathogenesis and potential therapeutic targets.

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