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

Journal of Molecular Signaling

László Buday³  Miklós Geiszt¹  Zalán Péterfi²  Szabolcs Pesti³  Gábor Bőgel³  Anna Fekete⁴ 

[1] “Lendület” Peroxidase Enzyme Research Group of the Semmelweis University and the Hungarian Academy of Sciences, Budapest 1094, Hungary;Department of Physiology, Semmelweis University Medical School, Budapest, Hungary;Department of Medical Chemistry, Semmelweis University Medical School, Budapest 1094, Hungary;Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1113, Hungary

关键词: Src;    PI 3-kinase;    PX domain;    Tks4;    Tks5;    EGF receptor;   

Others  :  802507
DOI  :  10.1186/1750-2187-8-8

 received in 2013-01-16, accepted in 2013-08-06,  发布年份 2013

【 摘 要 】

Background

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.

Results

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.

Conclusions

Our results identify Tks5 as a novel component of the EGF signaling pathway.

【 授权许可】

   
2013 Fekete et al.; licensee BioMed Central Ltd.

【 图 表 】

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