Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Cell Cycle Proteins*
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Cell Line
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DNA, Complementary
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GTP-Binding Proteins / metabolism*
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Guanosine Triphosphate / metabolism*
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins / metabolism
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Mice
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Molecular Sequence Data
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Protein Binding
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Protein Serine-Threonine Kinases*
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Proteins / chemistry
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Proteins / metabolism*
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Signal Transduction
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rac GTP-Binding Proteins
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ras Proteins
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rho GTP-Binding Proteins*
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rhoA GTP-Binding Protein
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rhoB GTP-Binding Protein
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rhoC GTP-Binding Protein
Substances
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Cell Cycle Proteins
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DNA, Complementary
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Proteins
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Guanosine Triphosphate
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citron-kinase
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Protein Serine-Threonine Kinases
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GTP-Binding Proteins
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Rhoc protein, mouse
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rac GTP-Binding Proteins
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ras Proteins
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rho GTP-Binding Proteins
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rhoA GTP-Binding Protein
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rhoB GTP-Binding Protein
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rhoC GTP-Binding Protein