GTP binding proteins and growth factor signal transduction

1991 ◽  
Vol 3 (6) ◽  
pp. 491-499 ◽  
Author(s):  
Harlan E. Ives
1989 ◽  
Vol 185 (3) ◽  
pp. 347-355 ◽  
Author(s):  
Katsuhiko Yamamoto ◽  
Tetsuji Tanimoto ◽  
Shigekuni Kim ◽  
Akira Kikuchi ◽  
Yoshimi Takai

1996 ◽  
Vol 315 (3) ◽  
pp. 775-779 ◽  
Author(s):  
Gary M. BOKOCH ◽  
Chris J. VLAHOS ◽  
Yan WANG ◽  
Ulla G. KNAUS ◽  
Alexis E. TRAYNOR-KAPLAN

The Rac GTP-binding proteins are members of the Rho family and regulate growth factor-stimulated actin assembly in a variety of cells. The formation of phosphorylated inositol lipids has been implicated in control of the processes initiating and regulating such actin polymerization. Associations of Rho family GTP-binding proteins with enzymes involved in lipid metabolism have been described. Here we demonstrate a direct and specific interaction of Rac proteins with phosphatidylinositol (PI) 3-kinase. This interaction is dependent upon Rac being in a GTP-bound state and requires an intact Rac effector domain. In contrast, direct binding of RhoA to PI 3-kinase could not be detected. Rac–GTP also bound to PI 3-kinase in Swiss 3T3 fibroblast and human neutrophil lysates, and increased PI 3-kinase activity became associated with Rac–GTP in platelet-derived growth factor-stimulated cells. Interaction of Rac–GTP with PI 3-kinase in vitro stimulated the activity of the enzyme by 2–9-fold. A specific interaction of active Rac with PI 3-kinase might be important in regulation of the actin cytoskeleton.


2009 ◽  
pp. 81-129
Author(s):  
Bastien D. Gomperts ◽  
IJsbrand M. Kramer ◽  
Peter E.R. Tatham

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