NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases
Copyright policy )NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases
Cullin proteins assemble a large number of RING E3 ubiquitin ligases and regulate various physiological processes. Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases through an as yet undefined mechanism. We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary complex with CUL1 and ROC1. CAND1 dissociated SKP1 from CUL1 and inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the level of the CUL1-SKP1 complex. We suggest that by restricting SKP1-CUL1 interaction, CAND1 regulated the assembly of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be utilized by a large number of SKP1-F box-substrate subcomplexes.
- University of North Carolina at Chapel Hill United States
- Kyoto University Japan
- UNC Lineberger Comprehensive Cancer Center United States
SKP Cullin F-Box Protein Ligases, NEDD8 Protein, Macromolecular Substances, F-Box Proteins, Molecular Sequence Data, Genes, myc, Cell Cycle Proteins, Cell Biology, Saccharomyces cerevisiae, Cullin Proteins, Recombinant Proteins, DNA-Binding Proteins, Ligases, Kinetics, Bacterial Proteins, Mutagenesis, Site-Directed, Humans, Amino Acid Sequence, Enzyme Inhibitors, Peptide Synthases, Carrier Proteins, Molecular Biology
SKP Cullin F-Box Protein Ligases, NEDD8 Protein, Macromolecular Substances, F-Box Proteins, Molecular Sequence Data, Genes, myc, Cell Cycle Proteins, Cell Biology, Saccharomyces cerevisiae, Cullin Proteins, Recombinant Proteins, DNA-Binding Proteins, Ligases, Kinetics, Bacterial Proteins, Mutagenesis, Site-Directed, Humans, Amino Acid Sequence, Enzyme Inhibitors, Peptide Synthases, Carrier Proteins, Molecular Biology
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