Massive Actin Polymerization Induced by Phosphatidylinositol-4-phosphate 5-Kinasein Vivo

Yoshikazu Shibasaki, Hisamitsu Ishihara, Nobuaki Kizuki, Tomoichiro Asano, Yoshitomo Oka, Yoshio Yazaki
1997 Journal of Biological Chemistry  
The Rho family GTP-binding proteins have been known to mediate extracellular signals to the actin cytoskeleton. Although several Rho interacting proteins have been found, downstream signals have yet to be determined. Many actin-binding proteins are known to be regulated by phosphatidylinositol 4,5-bisphosphate in vitro. Rho has been shown to enhance the activity of phosphatidylinositol-4-phosphate 5-kinase (PI4P5K), the phosphatidylinositol 4,5-bisphosphate synthesizing enzyme. Recently we
more » ... e. Recently we isolated several isoforms of type I PI4P5K. Here we report that PI4P5K I␣ induces massive actin polymerization resembling "pine needles" in COS-7 cells in vivo. When truncated from the C terminus to amino acid 308 of PI4P5K I␣, both kinase activity and actin polymerizing activity were lost. Although the dominant negative form of Rho, RhoN19, alone decreased actin fibers, those induced by PI4P5K were not affected by the coexpression of RhoN19. These results suggest that PI4P5K is located downstream from Rho and mediates signals for actin polymerization through its phosphatidylinositol-4-phosphate 5-kinase activity.
doi:10.1074/jbc.272.12.7578 pmid:9065410 fatcat:ncvbid74z5gwdimajvbkaogfze