Cited by 447HER2/EGFR in Cancer ResearchFibroblast Growth Factor ResearchCytokine Signaling Pathways and Interactions

The epidermal growth factor receptor ligands at a glance

Schneider, Marlon R., Wolf, Eckhard·2009·Journal of Cellular Physiology

Abstract

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.

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Crossref · 10.1002/jcp.21635

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  • Human recombinant HB-EGF consists of amino acids 1-148 of pro-HB-EGF, a membrane-spanning protein that sheds its ectodomain to release a soluble EGF-like domain that binds EGFR.

    “Human recombinant HB-EGF is encoded by amino acids 1–148 of pro-HB-EGF which is a membrane spanning protein that undergoes ectodomain shedding, releasing a soluble extracellular portion that contains an EGF-like domain that binds the EGFR”

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Authors
Schneider, M. R., & Wolf, E.
Affiliations
Ludwig-Maximilians-Universität München (DE)
Corresponding author
Schneider, Marlon R.
Venue
Journal of Cellular Physiology
Publisher
Wiley
Published
2008-11-12
Volume
218
Issue
3
Pages
460-466
ISSN
  • 0021-9541 (ISSN-L)
  • 1097-4652
OpenAlex
W1992913621
Cited by
447
References
102
Citations by year
2026: 9 · 2025: 11 · 2024: 28 · 2023: 24 · 2022: 24 · 2021: 22 · 2020: 23 · 2019: 23 · 2018: 27 · 2017: 27 · 2016: 19 · 2015: 31 · 2014: 50 · 2013: 28 · 2012: 26
FWCI
2.22
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Cellular Physiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Deutsche Forschungsgemeinschaft
Topics
  • Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
  • Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Keywords
epidermal growth factor receptor, EGF ligands, juxtacrine signaling, ectodomain shedding, soluble growth factors, transmembrane proteins, cell proliferation, tissue homeostasis, carcinogenesis, development (biology)
MeSH terms
Amino Acid Sequence, Animals, Humans, Ligands, Molecular Sequence Data, Structure-Activity Relationship, Evolution, Molecular, ErbB Receptors

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