Abstract
A miniaturized, bead-based protein-protein-interaction assay was developed to study the interaction of Rho GTPases with regulatory proteins. The setup, which uses only minute amounts of sample, was used to analyze small molecules that inhibit the interaction between Rho GTPases and RhoGDI alpha. Prenylcysteine analogues and the replacement of GDP by non-hydrolysable GTP analogues prevented the formation of Rho GTPase-RhoGDI alpha complexes in a concentration-dependent manner.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Enzyme Activation
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Guanine Nucleotide Dissociation Inhibitors / analysis*
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Guanine Nucleotide Dissociation Inhibitors / metabolism
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Protein Binding
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Proteomics / methods*
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rho GTP-Binding Proteins / analysis*
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rho GTP-Binding Proteins / antagonists & inhibitors
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rho GTP-Binding Proteins / metabolism
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rho-Specific Guanine Nucleotide Dissociation Inhibitors
Substances
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Guanine Nucleotide Dissociation Inhibitors
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rho-Specific Guanine Nucleotide Dissociation Inhibitors
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rho GTP-Binding Proteins