Adhesion-dependent tyrosine phosphorylation of enabled in Drosophila neuronal cell line

被引：5

作者：

Takagi, Y

Ui-Tei, K

Hirohashi, S

机构：

[1] Nippon Med Sch, Dept Pharmacol, Tokyo, Japan

[2] Natl Canc Ctr, Div Pathol, Res Inst, Tokyo, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 270卷 / 02期

关键词：

D O I：

10.1006/bbrc.2000.2458

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cell. culture consisting of Drosophila BG2-c6 cells and laminin revealed its value for the analysis of the integrin-mediated activity of extracellular matrix (Takagi, Y., et al, (1998) Neurosci. Lett, 244, 149-152), To elucidate Drosophila integrin cascade further, we report here our characterization on the tyrosine phosphorylation in BG2-c6 cells, coupling with their spreading on extracellular matrix. Large-scale culture of Drosophila Kc167 cells provided a sufficient amount of extracellular matrix (including laminin) for performing biochemical analysis on the signal transduction in BG2-c6 cells. Several proteins underwent significant tyrosine phosphorylation in an adhesion dependent manner. Among them, the heavy phosphorylation of Enabled (a substrate for Abelson tyrosine kinase) was noteworthy because of the proposed function of Enabled in cell adhesion. Together with our previous results, we propose a model for signal transduction activated by cell adhesion for the first time in Drosophila. 2000 Academic Press.

引用

页码：482 / 487

页数：6

共 20 条

[1] Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1) and EVH2 domains [J].