The epidermal growth factor receptor ligands at a glance
Version of Record online: 12 NOV 2008
Copyright © 2008 Wiley-Liss, Inc.
Journal of Cellular Physiology
Volume 218, Issue 3, pages 460–466, March 2009
How to Cite
Schneider, M. R. and Wolf, E. (2009), The epidermal growth factor receptor ligands at a glance. J. Cell. Physiol., 218: 460–466. doi: 10.1002/jcp.21635
- Issue online: 18 DEC 2008
- Version of Record online: 12 NOV 2008
- Manuscript Accepted: 7 OCT 2008
- Manuscript Received: 4 JUN 2008
- Deutsche Forschungsgemeinschaft. Grant Number: GRK 1029
The epidermal growth factor receptor (EGFR) regulates key processes of cell biology, including proliferation, survival, and differentiation during development, tissue homeostasis, and tumorigenesis. Canonical EGFR activation involves the binding of seven peptide growth factors. These ligands are synthesized as transmembrane proteins comprising an N-terminal extension, the EGF module, a short juxtamembrane stalk, a hydrophobic transmembrane domain, and a carboxy-terminal fragment. The central structural and functional feature is the EGF module, a sequence containing six cysteines in a conserved spacement which is responsible for binding to the EGFR. While the membrane-anchored peptide can be biologically active by juxtacrine signaling, in most cases the EGF module is proteolytically cleaved (a process termed ectodomain shedding) to release the soluble growth factor, which may act in an endocrine, paracrine, or autocrine fashion. This review summarizes the structural and functional properties of these fascinating molecules and presents selected examples to illustrate their roles in development, physiology, and pathology. J. Cell. Physiol. 218: 460–466, 2009. © 2008 Wiley-Liss, Inc.