EGF regulates tyrosine phosphorylation and membrane-translocation of the scaffold protein Tks5

Tks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells. Recent data have suggested that a close homologue of Tks5, Tks4, is im...

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Bibliographic Details
Published in:Journal of molecular signaling 2013-08, Vol.8 (1), p.8-8
Main Authors: Fekete, Anna, Bőgel, Gábor, Pesti, Szabolcs, Péterfi, Zalán, Geiszt, Miklós, Buday, László
Format: Article
Language:English
Subjects:
Cytoskeleton
Epidermal growth factor
Kinases
Microscopy
Phosphorylation
Proteins
Zebrafish
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Summary:Tks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells. Recent data have suggested that a close homologue of Tks5, Tks4, is implicated in the EGF signaling. Here, we report that Tks5 is a component of the EGF signaling pathway. In EGF-treated cells, Tks5 is tyrosine phosphorylated within minutes and the level of phosphorylation is sustained for at least 2 hours. Using specific kinase inhibitors, we demonstrate that tyrosine phosphorylation of Tks5 is catalyzed by Src tyrosine kinase. We show that treatment of cells with EGF results in plasma membrane translocation of Tks5. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutation of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks5. Our results identify Tks5 as a novel component of the EGF signaling pathway.
ISSN:1750-2187
1750-2187
DOI:10.1186/1750-2187-8-8