The epidermal growth factor

Details

Serval ID
serval:BIB_9DD869673175
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Title
The epidermal growth factor
Journal
Cell Biology International
Author(s)
Boonstra J., Rijken P., Humbel B, Cremers F, Verkleij A., van Bergen en Henegouwen
ISSN
1065-6995
Publication state
Published
Issued date
1995
Volume
19
Number
5
Pages
413-430
Language
english
Abstract
Epidermal growth factor (EGF) is a single polypeptide of 53 amino acid residues which is involved in the regulation of cell proliferation. Egf exerts its effects in the target cells by binding to the plasma membrane located EGF receptor. The EGF receptor is a transmembrane protein tyrosine kinase. Binding of EGF to the receptor causes activation of the kinase and subsequently receptor autophosphorylation. The autophosphorylation is essential for the interaction of the receptor with its substrates. These bind to the receptor by the so-called SH2 domains.
The signal transduction pathways activated by EGF include the phosphatidylinositol pathway, leading to activation of protein kinase C and to increase in the intracellular Ca2+ concentration, and to the ras pathway leading to MAP kinase activation.
Recently the cytoplasm has been implicated as playing an important role in EGF induced signal transduction. The EGF receptor has been demonstrated to be an actin-binding protein. In addition EGF causes a rapid actin depolymerisation and the formation of membrane ruffles. In particular these membrane ruffles have been shown to act as the first site of signal transduction after EGF binding, and thus may be considered as signal transduction structures. Finally evidence has been presented suggesting a positive role for EGF and/or the receptor in the nucleus.
Keywords
Epidermal Growth Factor (EGF), Epidermal Growth Factor Receptor (EGFR), Tyrosine Kinase (TK), Signal transduction, Cytoskeleton, SH2, SH3
Web of science
Create date
18/10/2012 13:52
Last modification date
20/08/2019 15:04
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