A novel partner for the GTP‐bound forms of rho and rac
Copyright policy )A novel partner for the GTP‐bound forms of rho and rac
Using the yeast two hybrid system and overlay assays we identified a putative rho/rac effector, citron, which interacts with the GTP‐bound forms of rho and rac1, but not with cdc42. Extensive homologies to known proteins were not observed. This 183 kDa protein contains a C6H2 zinc finger, a PH domain, and a long coiled‐coil forming region including 4 leucine zippers and the rho/rac binding site. We recently identified three others putative rho effectors characterized by a common rho binding motif. Citron does not share this motif and displays a distinctive protein organization, thus defining a separate class of rho partners.
- Kyoto University Japan
rho GTP-Binding Proteins, Two hybrid system, DNA, Complementary, Molecular Sequence Data, Cell Cycle Proteins, Signal transduction, Protein Serine-Threonine Kinases, Cell Line, Small GTP-binding protein, Mice, GTP-Binding Proteins, Zinc finger, Animals, Coiled-coil, Amino Acid Sequence, Pleckstrin homology, Binding Sites, Base Sequence, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Proteins, rac GTP-Binding Proteins, ras Proteins, Guanosine Triphosphate, Protein Binding, Signal Transduction
rho GTP-Binding Proteins, Two hybrid system, DNA, Complementary, Molecular Sequence Data, Cell Cycle Proteins, Signal transduction, Protein Serine-Threonine Kinases, Cell Line, Small GTP-binding protein, Mice, GTP-Binding Proteins, Zinc finger, Animals, Coiled-coil, Amino Acid Sequence, Pleckstrin homology, Binding Sites, Base Sequence, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Proteins, rac GTP-Binding Proteins, ras Proteins, Guanosine Triphosphate, Protein Binding, Signal Transduction
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