Abstract
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.
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