FEBS Letters · 1995 · 166 citations · 21 references
Life SciencesCell BiologyMolecular BiologyCell SignalingMolecular Cell BiologyProtein-protein InteractionsLigand BindingMacromolecular AssemblyProtein Complex AnalysisProtein Interaction DomainsProtein StructureProtein-protein RecognitionCoiled-coil DomainsCoiled-coil MotifsLeucine ZippersPh DomainsRho Family GtpasesZinc Finger DomainsZinc Finger MotifsZinc Finger Proteins
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.
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Predicting Coiled Coils from Protein Sequences
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The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
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