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 rholrac 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 rholrac 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.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Cycle Proteins, Cell Line, DNA, Complementary, GTP-Binding Proteins, Guanosine Triphosphate, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Mice, Molecular Sequence Data, Protein Binding, Protein-Serine-Threonine Kinases, Proteins, Signal Transduction, rac GTP-Binding Proteins, ras Proteins, rho GTP-Binding Proteins, rhoA GTP-Binding Protein, rhoB GTP-Binding Protein
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Cycle Proteins, Cell Line, DNA, Complementary, GTP-Binding Proteins, Guanosine Triphosphate, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Mice, Molecular Sequence Data, Protein Binding, Protein-Serine-Threonine Kinases, Proteins, Signal Transduction, rac GTP-Binding Proteins, ras Proteins, rho GTP-Binding Proteins, rhoA GTP-Binding Protein, rhoB GTP-Binding Protein
FEBS Lett.
Date: Dec. 18, 1995
PubMed ID: 8543060
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