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

Cell. culture consisting of Drosophila BG2-c6 cells and laminin revealed it s value for the analysis of the integrin-mediated activity of extracellular matrix (Takagi, Y., et al, (1998) Neurosci. Lett, 244, 149-152), To elucid ate Drosophila integrin cascade further, we report here our characterizatio n on the tyrosine phosphorylation in BG2-c6 cells, coupling with their spre ading on extracellular matrix. Large-scale culture of Drosophila Kc167 cell s provided a sufficient amount of extracellular matrix (including laminin) for performing biochemical analysis on the signal transduction in BG2-c6 ce lls. 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 pr oposed function of Enabled in cell adhesion. Together with our previous res ults, we propose a model for signal transduction activated by cell adhesion for the first time in Drosophila. 2000 Academic Press.