The epidermal growth factor

Détails

ID Serval
serval:BIB_9DD869673175
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
The epidermal growth factor
Périodique
Cell Biology International
Auteur⸱e⸱s
Boonstra J., Rijken P., Humbel B, Cremers F, Verkleij A., van Bergen en Henegouwen
ISSN
1065-6995
Statut éditorial
Publié
Date de publication
1995
Volume
19
Numéro
5
Pages
413-430
Langue
anglais
Résumé
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.
Mots-clé
Epidermal Growth Factor (EGF), Epidermal Growth Factor Receptor (EGFR), Tyrosine Kinase (TK), Signal transduction, Cytoskeleton, SH2, SH3
Web of science
Création de la notice
18/10/2012 14:52
Dernière modification de la notice
20/08/2019 16:04
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