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XD Ren, GM Bokoch, A Traynor-Kaplan, GH Jenkins, RA Anderson and MA Schwartz
Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037, USA.
Our previous work showed that post-translationally modified Rho in its GTP-bound state stimulated phosphatidylinositol 4-phosphate 5-kinase (PIP5K) activity in mouse fibroblast lysates. To investigate whether Rho physically interacts with PIP5K, we incubated immobilized Rho-GST with Swiss 3T3 cell lysates and tested for retained PIP5K activity. Rho- GST, but not Ras-GST or GST alone, bound significant PIP5K activity. The binding of PIP5K was independent of whether Rho was in a GTP- or GDP-bound state. An antibody against a 68-kDa human erythrocyte type I PIP5K recognized a single 68-kDa protein eluted from Rho-GST column. The Rho-associated PIP5K responded to phosphatidic acid differentially from the erythrocyte type I PIP5K, suggesting that it could be a distinct isoform not reported previously. Rho co-immunoprecipitated with the 68-kDa PIP5K from Swiss 3T3 lysates, demonstrating that endogenous Rho also interacts with PIP5K. ADP-ribosylation of Rho with C3 exoenzyme enhanced PIP5K binding by approximately eightfold, consistent with the ADP-ribosylated Rho functioning as a dominant negative inhibitor. These results demonstrate that Rho physically interacts with a 68-kDa PIP5K, although whether the association is direct or indirect is unknown.
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V. Martel, C. Racaud-Sultan, S. Dupe, C. Marie, F. Paulhe, A. Galmiche, M. R. Block, and C. Albiges-Rizo Conformation, Localization, and Integrin Binding of Talin Depend on Its Interaction with Phosphoinositides J. Biol. Chem., June 8, 2001; 276(24): 21217 - 21227. [Abstract] [Full Text] [PDF]
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Nour.-E.-H. Chatah and C. S. Abrams G-protein-coupled Receptor Activation Induces the Membrane Translocation and Activation of Phosphatidylinositol-4-phosphate 5-Kinase Ialpha by a Rac- and Rho-dependent Pathway J. Biol. Chem., August 31, 2001; 276(36): 34059 - 34065. [Abstract] [Full Text] [PDF]
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