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The small GTP-binding protein rac regulates growth factor-induced membrane ruffling.
The function of rac, a ras-related GTP-binding protein, was investigated in fibroblasts by microinjection. In confluent serum-starved Swiss 3T3 cells, rac1 rapidly stimulated actin filament accumulation at the plasma membrane, forming membrane ruffles. Several growth factors and activated H-ras also induced membrane ruffling, and this response was prevented by a dominant inhibitory mutant rac protein, N17rac1. This suggests that endogenous rac proteins are required for growth factor-induced membrane ruffling. In addition to membrane ruffling, a later response to both rac1 microinjection and some growth factors was the formation of actin stress fibers, a process requiring endogenous rho proteins. Using N17rac1 we have shown that these growth factors act through rac to stimulate this rho-dependent response. We propose that rac and rho are essential components of signal transduction pathways linking growth factors to the organization of polymerized actin.
Institute for Cancer Research, Chester Beatty Laboratories, London, England., , ,
Culture Media, Serum-Free
Fluorescent Antibody Technique
Oncogene Protein p21(ras)
rac GTP-Binding Proteins
Pub Type(s)Journal Article
Research Support, Non-U.S. Gov't